M Trudel

Publications of M Trudel

• Complete protection of mice from respiratory syncytial virus infection following mucosal delivery of synthetic peptide vaccines.

  Authors: N Bastien, M Trudel, C Simard

  Vaccine. 03/1999; 17(7-8):832-6.

  We have previously shown that intraperitoneal immunization of BALB/c mice with the 14 amino-acid long synthetic peptides G/174-187 and BG/174-187, representing the region 174-187 of theWe have previously shown that intraperitoneal immunization of BALB/c mice with the 14 amino-acid long synthetic peptides G/174-187 and BG/174-187, representing the region 174-187 of the G-glycoprotein from human (H) and bovine (B) respiratory syncytial virus (RSV), respectively, completely protects animals from infection with the corresponding virus. A current goal in vaccine development being the delivery of noninvasive protective antigens via mucosal surfaces, we have evaluated the immunogenicity and protective efficacy of the two peptides when administered to mice by the intranasal (i.n.) route in the presence or absence of the cholera toxin (CT) as a mucosal adjuvant. The two peptides given alone induced the production of RSV-specific circulating IgG, as revealed by ELISA titers of immune sera. When the peptides were administered intranasally with CT, the higher IgG antibody titer which was induced was within the same order of magnitude as that obtained following i.n. immunization with live RSV or intraperitoneal injection with the peptides, thus demonstrating the stimulatory effect of the CT adjuvant. Moreover, although the peptides fail to induce a detectable level of secretory IgA, all animals immunized i.n. with peptide BG/174-187 (plus or minus CT) and all those immunized with peptide G/174-187 mixed with CT were completely resistant to infection by the corresponding virus. To our knowledge, this is the first study reporting that complete protection against a natural pathogen can be elicited by mucosally delivered synthetic peptides. This supports the usefulness of synthetic peptides in prophylactic vaccination.

• Protective immune responses induced by the immunization of mice with a recombinant bacteriophage displaying an epitope of the human respiratory syncytial virus.

  Authors: N Bastien, M Trudel, C Simard

  Virology. 08/1997; 234(1):118-22.

  We investigated whether a recombinant bacteriophage displaying a disease-specific protective epitope could be experimentally used as a vaccine to confer protection of immunized animals againstWe investigated whether a recombinant bacteriophage displaying a disease-specific protective epitope could be experimentally used as a vaccine to confer protection of immunized animals against infection. We genetically engineered a recombinant phage, fd, displaying at its surface a chimeric pIII coat protein fused to the previously identified protective epitope 173-187 from the glycoprotein G of the human respiratory syncytial virus (RSV). A selected recombinant fd phage elicited a strong immune response in mice, inducing a high level of circulating RSV-specific antibodies. Mice immunized with the recombinant phage acquired a complete resistance to RSV infection as evidenced by the lack of detectable virus particles in their lungs following intranasal challenge with live RSV. In contrast, a high level of virus particles was found in the lungs of either animals immunized with the wild-type fd phage or nonimmunized mice. To our knowledge, this is the first study to report the ability of a phage presenting an immunogenic peptide to prevent infection of immunized animals by a pathogen. This finding should facilitate the identification of pathogen-specific protective epitopes selected from random phage peptide libraries, as it is simpler and less expensive than the conventional method of synthesis and coupling of phage-specific peptide ligand sequences for immunization.

• Subgroup specific protection of mice from respiratory syncytial virus infection with peptides encompassing the amino acid region 174-187 from the G glycoprotein: the role of cysteinyl residues in protection.

  Authors: C Simard, F Nadon, C Séguin, N N Thien, H Binz, J Basso, J F Laliberté, M Trudel

  Vaccine. 03/1997; 15(4):423-32.

  We identified subgroup specific protective epitopes represented by the amino acid regions 174-187 and 171-187 of the G glycoproteins from respiratory syncytial virus (RSV), subgroups A and B. MiceWe identified subgroup specific protective epitopes represented by the amino acid regions 174-187 and 171-187 of the G glycoproteins from respiratory syncytial virus (RSV), subgroups A and B. Mice immunized with coupled synthetic peptides corresponding to either the region 174-187 containing a Cys186-->Ser substitution or to the native region 171-187 were completely resistant to RSV infection but only to the respective virus. The protective activities of the peptides 174-187 were dependent on the Cys186-->Ser substitution. In addition, a recombinant protein representing the region 125-203 of the A subgroup G glycoprotein expressed in Escherichia coli was capable without further treatment to completely protect animals against RSV subgroup A infection. We show that the combinations of cysteinyl residues (positions 173, 176, 182, and 186) retained within either synthetic peptides or the recombinant protein G125-203 greatly influenced their protective activities. This indicates that the region 171-187 is essential for the protection conferred by the G125-203 protein. Furthermore, our results strongly suggest that the peptides' and recombinant protein's potencies are a function of a loop-like structure which is stabilized by intramolecular disulfide linkages between Cys176-Cys182 and Cys173-Cys186. This is further supported by the observation that chemical blocking of the sulfidryl groups in synthetic peptides completely eliminated their protective activity.

• Transcriptional and translational expression kinetics of the early gene encoding the BICP27 protein of bovine herpesvirus type 1.

  Authors: A Chalifour, J Basso, N Gagnon, M Trudel, C Simard

  Virology. 11/1996; 224(1):326-9.

  The expression kinetics of an essential trans-regulatory protein, ICP27, from herpes simplex virus type 1 correspond to that of an immediate-early gene whose expression increases rapidly uponThe expression kinetics of an essential trans-regulatory protein, ICP27, from herpes simplex virus type 1 correspond to that of an immediate-early gene whose expression increases rapidly upon infection and then decreases as of 7 hr postinfection. In contrast, here we report that the bovine herpesvirus type 1 (BHV-1) homolog BICP27, a 50-kDa protein, is expressed as an early gene. Both the transcript and protein accumulated gradually reaching peak levels at approximately 12 hr postinfection, after which point steady state levels were maintained up to 24 hr. Thus the expression profiles of ICP27 and BICP27 are significantly different, suggesting that they may possess different functions.

• The bovine herpesvirus type 1 major tegument protein VP8 expressed in recombinant vaccinia virus does not induce significant immunity in mice.

  Authors: S LaBoissière, M Trudel, C Simard

  Virus research. 03/1996; 40(2):191-8.

  We previously reported the characterization of the gene encoding the bovine herpesvirus type 1 (BHV-1) major tegument protein VP8. With the aim of defining the immunological properties of thisWe previously reported the characterization of the gene encoding the bovine herpesvirus type 1 (BHV-1) major tegument protein VP8. With the aim of defining the immunological properties of this protein, we constructed a recombinant vaccinia virus (VV-VP8) in which expression of the VP8 gene was regulated by the P7.5 early/late promoter. Since the sequence of the VP8 gene contained a TTTTTNT motif known to serve as a transcription termination signal of vaccinia virus genes of the early class, a second recombinant (VV-VP8-Mut) in which this signal was modified by site-directed mutagenesis was created. Characterization of the recombinant viruses revealed that truncated VP8 mRNA and protein (69 kDa) were synthesized in VV-VP8 infected cells, whereas cells infected with VV-VP8-Mut produced a protein which was undistinguishable from that of the BHV-1 encoded protein (92-94 kDa). Immunization of BALB/c mice (H-2d) with VV-VP8-Mut induced a low VP8-specific antibody response whereas no specific response was induced in VV-VP8 inoculated mice. The low humoral response elicited was similar in C57BL/6 (H-2b) and C3H (H-2k) mice. Furthermore, immunization of mice with VV-VP8-Mut did not induce a BHV-1-specific lymphoproliferation in the three mice strains examined. Our results contrast with a recent study showing that immunization of calves with purified VP8 stimulated both T cell proliferation and antibody production.

• Evidence that the amino acid region 124-203 of glycoprotein G from the respiratory syncytial virus (RSV) constitutes a major part of the polypeptide domain that is involved in the protection against RSV infection.

  Authors: C Simard, F Nadon, C Séguin, M Trudel

  Antiviral research. 01/1996; 28(4):303-15.

  The first 230 residues of the 298-amino acid glycoprotein G of respiratory syncytial virus (RSV) are sufficient to confer complete resistance to challenge with live RSV, whereas the first 180The first 230 residues of the 298-amino acid glycoprotein G of respiratory syncytial virus (RSV) are sufficient to confer complete resistance to challenge with live RSV, whereas the first 180 residues completely failed (Olmsted et al. (1989) J. Virol. 63, 411-420). The characterization of a protective epitope corresponding to the amino acid region 174-187 of the G protein (Trudel et al. (1991) Virology 185, 749-757) suggests that interruption of this region in the 180 residue truncated polypeptide may be responsible for its inability to confer protection and consequently that the 174-187 region may play a major role in the protection effected by the protein G. To support these hypotheses, we examined the ability of the amino acid region 124-203 of glycoprotein G to confer protection. The corresponding peptide was expressed as a non-fusion protein in a recombinant vaccinia virus designated VG27. Immunization of BALB/c mice with this recombinant efficiently induced the production of antibodies capable of recognizing both the parental glycoprotein G and peptide 174-187. Furthermore, upon challenge with RSV, a significant decrease of infectious particles was found in the lungs of mice immunized with VG27 as compared with non-immunized mice. Our results suggest that the 124-203 amino acid region of the RSV G protein constitutes a major part of the domain involved in protection.

• Sequence analysis of the UL39, UL38, and UL37 homologues of bovine herpesvirus 1 and expression studies of UL40 and UL39, the subunits of ribonucleotide reductase.

  Authors: C Simard, I Langlois, D Styger, B Vogt, C Vlcek, A Chalifour, M Trudel, M Schwyzer

  Virology. 11/1995; 212(2):734-40.

  We sequenced the region of the bovine herpesvirus type 1 (BHV-1) genome corresponding to map units 0.172-0.230 (7964 bp), representing the UL39, UL38, and UL37 homologues of herpes simplex virusWe sequenced the region of the bovine herpesvirus type 1 (BHV-1) genome corresponding to map units 0.172-0.230 (7964 bp), representing the UL39, UL38, and UL37 homologues of herpes simplex virus which encode the large subunit of ribonucleotide reductase (RR) and components of the viral capsid and the tegument, respectively. To discriminate between two potential initiator AUGs of the UL39 gene, the 5' end of the mRNA was mapped by S1 nuclease protection assays. Comparison of the amino acid sequences of the three BHV-1 proteins with analogous polypeptides from several other herpesviruses revealed significant levels of homology. We also compared the expression kinetics of the large (R1, UL39) versus the small (R2, UL40) RR subunits during the course of in vitro BHV-1 infection by Western blotting using specifically developed and calibrated antisera. Our results show that the R1 protein was synthesized earlier than its R2 counterpart. Moreover, the R1 protein accumulated to a higher level than the R2 protein even though the R2 transcript was in greater abundance than the R1 mRNA. This is discussed with regard to the translational efficiency of their transcripts.

• Characterization and transcript mapping of a bovine herpesvirus type 1 gene encoding a polypeptide homologous to the herpes simplex virus type 1 major tegument proteins VP13/14.

  Authors: S LaBoissière, M Trudel, C Simard

  The Journal of general virology. 12/1992; 73 ( Pt 11):2941-7.

  Using in vitro translation of hybrid-selected mRNA, we have previously shown that bovine herpesvirus type 1 HindIII fragment M encodes an abundant 94K polypeptide. Using immunoprecipitation andUsing in vitro translation of hybrid-selected mRNA, we have previously shown that bovine herpesvirus type 1 HindIII fragment M encodes an abundant 94K polypeptide. Using immunoprecipitation and sequencing analyses, it has now been shown that the polypeptide is related to the major tegument protein VP8 and is homologous to the herpes simplex virus type 1 major tegument proteins VP13/14. The sequence of the VP8 gene (field isolate 34) is reported and compared to published data. Several differences between the sequences were detected, resulting particularly from base insertions/deletions generating three major frameshifts affecting an area of 87 amino acid residues of the encoded protein. In addition, sequence comparison revealed 29 single base alterations, excluding frameshift regions, producing 17 amino acid substitutions. Overall, 14.1% of the deduced amino acid sequences were divergent. We have also established that the last 152 nucleotides of the previously reported sequence correspond to the sequence of the minus not the sense strand. Finally, we report that the 4.4 kb transcript of the VP8 gene is initiated 39 nucleotides upstream from the translation start codon.

• Sequencing and 5'- and 3'-end transcript mapping of the gene encoding the small subunit of ribonucleotide reductase from bovine herpesvirus type-1.

  Authors: C Simard, N Bastien, M Trudel

  Virology. 11/1992; 190(2):689-701.

  The complete nucleotide sequence of the gene encoding the small subunit of ribonucleotide reductase (RNR) from bovine herpesvirus type-1 (BHV-1) was determined. The genomic DNA fragment sequencedThe complete nucleotide sequence of the gene encoding the small subunit of ribonucleotide reductase (RNR) from bovine herpesvirus type-1 (BHV-1) was determined. The genomic DNA fragment sequenced also represented regions corresponding to the carboxy termini of RNR large subunit and of a virion protein causing host shut-off. The small subunit polypeptide was constituted of 314 amino acid residues totalling 35.25 kDa. The major transcription initiation and termination sites of the small subunit mRNA were located 95 bases upstream and 88 nucleotides downstream from the coding region, respectively. These findings indicate that the mRNA was 1128 bases long which correlated well with the size of the polyadenylated transcript detected in Northern blot analysis (1.3 kb). Within the RNR large subunit coding region, a TATA box and two CAAT box motifs were found 26, 104, and 190 nucleotides, respectively, upstream from the transcription initiation site of the small subunit mRNA. In contrast to previous studies (Slabaugh et al., J. Virol. 1988, 62, 519-527; Boursnell et al., Virology 1991, 184, 411-416), our comparative analysis of five herpesviruses, one iridovirus, and one poxvirus small subunit protein sequences suggested that the seven viruses arose from a common lineage.

• Initiation of cytotoxic T-cell response and protection of Balb/c mice by vaccination with an experimental ISCOMs respiratory syncytial virus subunit vaccine.

  Authors: M Trudel, F Nadon, C Séguin, S Brault, Y Lusignan, S Lemieux

  Vaccine. 02/1992; 10(2):107-12.

  Respiratory syncytial virus is an important human pathogen causing serious lower respiratory tract infections of children and elderly people. Previous studies on the development of experimentalRespiratory syncytial virus is an important human pathogen causing serious lower respiratory tract infections of children and elderly people. Previous studies on the development of experimental subunit vaccines either expressed by recombinant DNA technology or prepared from purified viral proteins absorbed on adjuvant (ISCOMs) have shown promise. The present work reports on the effectiveness of an experimental ISCOMs vaccine in initiating humoral and cell-mediated immune responses and in providing overall protection upon live virus challenge in Balb/c mice; results indicate that vaccination by the intramuscular route is more effective, even if vaccination by the intranasal route also significantly reduced virus shedding.

• Protection of BALB/c mice from respiratory syncytial virus infection by immunization with a synthetic peptide derived from the G glycoprotein.

  Authors: M Trudel, F Nadon, C Séguin, H Binz

  Virology. 01/1992; 185(2):749-57.

  A synthetic peptide homologous to amino acids 174-187 of the G glycoprotein of the A2 strain of human respiratory syncytial (RS) virus (G/174-187) was shown to induce protection from live virusA synthetic peptide homologous to amino acids 174-187 of the G glycoprotein of the A2 strain of human respiratory syncytial (RS) virus (G/174-187) was shown to induce protection from live virus challenge of BALB/c mice after immunization with three doses of 50 micrograms of peptide coupled to keyhole limpet hemocyanin. Immunized mice showed high levels of circulating RS-specific antibodies as detected by ELISA assay; however, no neutralizing antibodies were found. Moreover, an important short-term cytotoxic T-cell response was observed with lymphocytes isolated from the lungs but not from the spleen of immunized mice. This response was lost 24 weeks after immunization; however, mice remained protected against challenge with live RS virus. In addition, a monoclonal antibody that specifically binds to peptide G/174-187 was found efficient in conferring passive protection from challenge: this data further supports our results on the importance of the 174-187 region in protection. Another peptide, spanning amino acids 144 to 159, was shown to induce neutralizing antibodies but did not confer protection.

• Synthetic peptides corresponding to the F protein of RSV stimulate murine B and T cells but fail to confer protection.

  Authors: M Trudel, E J Stott, G Taylor, D Oth, G Mercier, F Nadon, C Séguin, C Simard, M Lacroix

  Archives of virology. 02/1991; 117(1-2):59-71.

  We have previously located a major neutralization site of the fusion protein of respiratory syncytial virus (RSV) in the polypeptide region extending from amino acids Ile221 to Glu232. In thisWe have previously located a major neutralization site of the fusion protein of respiratory syncytial virus (RSV) in the polypeptide region extending from amino acids Ile221 to Glu232. In this report, 8 peptides corresponding to the six major hydrophilic regions of the F1 subunit were selected to analyse their immunogenic and protective capacities as well as their ability to block the high neutralization activities of 4 monoclonal antibodies (MAbs). Only 5 of the 8 peptides tested induced specific antibodies while all induced an in vitro interleukin-2 response of splenocytes from immunized mice. Peptide 3 (Ile221-Phe237) was able to elicit neutralizing antibodies, confirming our previous hypothesis concerning the location of a neutralization site. However, immunization with the latter did not induce significant reduction of virus in lungs of BALB/c mice upon challenge, probably due to an inadequate level of circulating neutralizing antibodies. Interestingly, peptides 2 (Asn216-Glu232), 3 (Ile221-Phe237), and 5 (Ser275-Ile288) blocked in vitro neutralization by four different F1 specific MAbs. A hypothesis is proposed to explain these results.

• Genomic heterogeneities in bovine herpesvirus type 1 viral isolates: a major variant selected from a field isolate.

  Authors: C Simard, S LaBoissière, C Séguin, M Trudel

  Intervirology. 02/1991; 32(3):117-26.

  We have analyzed viral DNA patterns, obtained following digestion of six different infectious bovine rhinotracheitis isolates, using a panel of restriction enzymes. Several differences in profilesWe have analyzed viral DNA patterns, obtained following digestion of six different infectious bovine rhinotracheitis isolates, using a panel of restriction enzymes. Several differences in profiles were observed, particularly for a Canadian viral strain which presumably contained a genome that was larger than the other five infectious bovine rhinotracheitis genomes. Also, an insertion/deletion of a HindIII restriction site was found in the DNA of a Danish strain; this additional HindIII site was localized precisely within the original HindIII E fragment of the infectious bovine rhinotracheitis virus. Interestingly, results could be used to distinguish each viral strain examined from the others by simple digestion with the appropriate enzyme.

• Gene mapping of infectious bovine rhinotracheitis viral DNA genome.

  Authors: C Simard, F Nadon, C Séguin, S LaBoissière, M Trudel

  Archives of virology. 02/1990; 110(1-2):63-75.

  A bovine herpesvirus I (BHV-I) HindIII genomic bank spanning 89% of the entire genome was constructed and individual fragments analyzed for their capacity to select specific mRNAs which were thenA bovine herpesvirus I (BHV-I) HindIII genomic bank spanning 89% of the entire genome was constructed and individual fragments analyzed for their capacity to select specific mRNAs which were then expressed by in vitro translation assays. This procedure allowed the mapping of more than 20 viral polypeptides to discrete regions of the DNA genome. Some polypeptides map in neighboring HindIII fragments while most seem encoded in single fragments. In particular, the coding sequences for an abundant 94 kDa polypeptide, which is the potential unglycosylated precursor of gII glycoprotein, have been assigned to the small 3.6 kbp HindIII genomic fragment M. The localization of structural and non-structural gene-coding sequences will help to characterize viral polypeptides and eventually, a better understanding of BHV-I infection will be gained.

• Concentration of Giardia lamblia cysts, Legionella pneumophila, Clostridium perfringens, human enteric viruses, and coliphages from large volumes of drinking water, using a single filtration.

  Authors: P Payment, A Bérubé, D Perreault, R Armon, M Trudel

  Canadian journal of microbiology. 11/1989; 35(10):932-5.

  Poliovirus, coliphages, Giardia lamblia cysts, Clostridium perfringens spores, and Legionella pneumophila were concentrated simultaneously in a single pass by sequential filtration of large volumesPoliovirus, coliphages, Giardia lamblia cysts, Clostridium perfringens spores, and Legionella pneumophila were concentrated simultaneously in a single pass by sequential filtration of large volumes of drinking water through 3- and 1-micron wound electronegative fiberglass cartridge filters (25.4 cm). Filtration was performed under acidic conditions (pH 3.5) in the presence of 0.001 M aluminum chloride to enhance adsorption. Elution of all the microorganisms entrapped or adsorbed to the filters was obtained by a slow backwash elution with a 1.5% beef extract solution, pH 9.75, containing 0.5% Tween 80. Tween 80 was shown to enhance recovery of the bacteriophages, bacteria, and parasites. Giardia cysts were efficiently eluted (71%) and could be reconcentrated by low-speed centrifugation and purified by sucrose density gradient flotation at a final recovery of 52%. Legionella pneumophila cells were eluted at 64% and were further concentrated by low-speed centrifugation at an overall recovery of 55%. C. perfringens spores and coliphages were eluted at efficiencies of 82 and 86%, respectively, and reconcentrated with minimal loss by a detergent - protein flotation method. Poliovirus was eluted at 93% and reconcentrated at 78% efficiency by organic flocculation.

• Rapid detection and identification of Legionella pneumophila by a membrane immunoassay.

  Authors: A Bérubé, M Trudel, P Payment

  Applied and environmental microbiology. 07/1989; 55(6):1640-1.

  Legionella pneumophila was detected and identified by an immunoblot assay using a monoclonal antibody specific to serogroups 1 to 8. Samples containing L. pneumophila were plated on buffered charcoalLegionella pneumophila was detected and identified by an immunoblot assay using a monoclonal antibody specific to serogroups 1 to 8. Samples containing L. pneumophila were plated on buffered charcoal yeast extract agar supplemented with glycine, vancomycin, and polymyxin B. After incubation at 35 degrees C for 3 days, colonies were transferred to nitrocellulose membranes by blotting. Simultaneous detection and identification of L. pneumophila were done by treating the membrane with the monoclonal antibody and a peroxidase conjugate to mouse immunoglobulins. A diffuse cross-reaction was observed with Pseudomonas fluorescens colonies, but this was a low-level reaction that could easily be differentiated from the strong specific reactions to L. pneumophila.

• Production and characterization of neutralizing monoclonal antibodies against poliovirus type 1, 2, and 3.

  Authors: P Payment, M Trudel, L Thibodeau, J Lecomte

  Canadian journal of microbiology. 06/1989; 35(5):550-3.

  Neutralizing monoclonal antibodies were produced against a reference vaccine or a reference wild strain of poliovirus type 1, 2, and 3. After 26 fusions, 55 monoclonal antibodies were obtained withNeutralizing monoclonal antibodies were produced against a reference vaccine or a reference wild strain of poliovirus type 1, 2, and 3. After 26 fusions, 55 monoclonal antibodies were obtained with serotype 1 as the immunizing antigen, 180 with serotype 2, and 115 with serotype 3. The neutralizing activity of these monoclonal antibodies was tested first with the two reference strains and then if reactive, against a panel of 10 well-characterized strains of each serotype, 5 vaccinelike (VL) and 5 nonvaccinelike (NVL). All monoclonal antibodies were type specific without reactivity with any of the heterologous strains. There was a wide range of reactivity within the strains of each serotype. Several monoclonal antibodies to serotype 1 reacted with all type 1 strains, while several neutralized strongly all VL strains and weakly one or more of the NVL strains. Most of the 180 monoclonal antibodies to serotype 2 neutralized to various degrees all strains of this serotype and about half reacted very strongly with all homologous strains whether VL or NVL. None could differentiate all VL and NVL homologous strains. Of the 115 monoclonal antibodies to serotype 3, several monoclonal antibodies neutralize to various levels all homologous strains and some can differentiate VL and NVL strains.

• Experimental polyvalent ISCOMs subunit vaccine induces antibodies that neutralize human and bovine respiratory syncytial virus.

  Authors: M Trudel, F Nadon, C Séguin, C Simard, G Lussier

  Vaccine. 03/1989; 7(1):12-6.

  The purpose of the present study was to evaluate experimentally, in guinea-pigs, the immunogenicity of respiratory syncytial (RS) virus subunit vaccines. Immunostimulating complexes (ISCOMs), madeThe purpose of the present study was to evaluate experimentally, in guinea-pigs, the immunogenicity of respiratory syncytial (RS) virus subunit vaccines. Immunostimulating complexes (ISCOMs), made from the surface proteins of both human (Long) and bovine (A-51908) RS strains adsorbed to the adjuvant Quil A, were assayed for their capacity to induce neutralizing antibodies, in comparison to experimental live virus vaccines. Serums from animals vaccinated with either the human or bovine RS subunit vaccines were equally efficient in neutralizing human or bovine RS virus. ISCOMs prepared with bovine RS virus proteins were significantly (p less than 0.05%) more efficient than their human counterpart, in inducing neutralizing antibodies, suggesting their greater potential as a subunit vaccine.

• Comparison of caprine, human and bovine strains of respiratory syncytial virus.

  Authors: M Trudel, F Nadon, C Simard, F Bélanger, R Alain, C Séguin, G Lussier

  Archives of virology. 02/1989; 107(1-2):141-9.

  A new continuous ovine kidney cell line allowing the growth of caprine, human and bovine respiratory syncytial virus was used to minimize host cell related variations for the direct comparison of theA new continuous ovine kidney cell line allowing the growth of caprine, human and bovine respiratory syncytial virus was used to minimize host cell related variations for the direct comparison of the viral ultrastructures, serological relationships and structural protein profiles. Results show that all three strains are closely related although a closer relationship was found between bovine and caprine RS.

• Control of infectious bovine rhinotracheitis in calves with a BHV-1 subunit-ISCOM vaccine.

  Authors: M Trudel, G Boulay, C Séguin, F Nadon, G Lussier

  Vaccine. 01/1989; 6(6):525-9.

  An ISCOM subunit vaccine was prepared by adsorption of purified viral membrane proteins of BHV-1 on the glycoside Quil A and assayed in six-month-old seronegative calves. Groups of five animals wereAn ISCOM subunit vaccine was prepared by adsorption of purified viral membrane proteins of BHV-1 on the glycoside Quil A and assayed in six-month-old seronegative calves. Groups of five animals were given three intramuscular doses of 50 or 25 micrograms BHV-1/ISCOMs or a commercial attenuated vaccine. Both types of vaccine induced seroconversion: the ISCOM vaccine consistently gave a serological response superior to that of the attenuated vaccine with maximal titres of 1/608 in haemagglutination inhibition and 1/53 in neutralization for the 50 micrograms dose compared to 1/152 haemagglutination units and 1/16 neutralizing titres for the attenuated vaccine. Calves vaccinated with the ISCOM vaccine were protected upon challenge whereas control animals showed signs of respiratory distress, and calves vaccinated with the attenuated vaccine developed only mild respiratory tract infection and mild increased rectal temperature. Virus shedding was reduced 100-fold in the attenuated vaccine group compared to 10,000-fold reduction in the ISCOM vaccine groups. The high level of protection induced indicates the potential of BHV-1/ISCOM as a subunit vaccine.