Furio Spano

Istituto Superiore di Sanità, Roma, Latium, Italy

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Publications (19)49.67 Total impact

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    ABSTRACT: Several lines of evidence demonstrated that organisms ranging from bacteria to higher animals possess a regulated endonucleolytic cleavage pathway producing half-tRNA fragments. In the present study, we investigated the occurrence of this phenomenon in two distantly-related apicomplexan parasites, Toxoplasma gondii, the agent of toxoplasmosis, and the rodent malaria parasite Plasmodium berghei. A low-scale molecular characterization of the small RNA fraction of T. gondii revealed the endonucleolytic processing of 10 distinct tRNA species, with cleavage in the anticodon loop and upstream of the 3'-terminal CCA sequence yielding 5'- or 3'-end half-tRNAs. T. gondii and P. berghei exhibited variable rates of tRNA cleavage upon egress from host cells and in response to stage differentiation, amino acid starvation and heat-shock. Moreover, avirulent isolates of T. gondii and attenuated P. berghei parasites showed a higher rate of tRNA cleavage than virulent strains. Interestingly, half-tRNA production was significantly higher in the metabolically quiescent bradyzoite and sporozoite stages of T. gondii, compared to the fast-growing tachyzoite. Collectively, our findings shed light for the first time on the occurrence of tRNA cleavage in apicomplexan parasites and suggest a relationship between half-tRNA production and growth rate in this important group of organisms.
    Molecular and Biochemical Parasitology 04/2013; · 2.73 Impact Factor
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    ABSTRACT: BACKGROUND: Toxoplasmosis is caused by the apicomplexan parasite Toxoplasma gondii and can be acquired either congenitally or via the oral route. In the latter case, transmission is mediated by two distinct invasive stages, i.e., bradyzoites residing in tissue cysts or sporozoites contained in environmentally resistant oocysts shed by felids in their feces. The oocyst plays a central epidemiological role, yet this stage has been scarcely investigated at the molecular level and the knowledge of its expressed proteome is very limited. RESULTS: Using one-dimensional gel electrophoresis coupled to liquid chromatography-linked tandem mass spectrometry, we analysed total or fractionated protein extracts of partially sporulated T. gondii oocysts, producing a dataset of 1304 non reduntant proteins (~18% of the total predicted proteome), ~59% of which were classified according to the MIPS functional catalogue database. Notably, the comparison of the oocyst dataset with the extensively covered proteome of T. gondii tachyzoite, the invasive stage responsible for the clinical signs of toxoplasmosis, identified 154 putative oocyst/sporozoite-specific proteins, some of which were validated by Western blot. The analysis of this protein subset showed that, compared to tachyzoites, oocysts have a greater capability of de novo amino acid biosynthesis and are well equipped to fuel the Krebs cycle with the acetyl-CoA generated through fatty acid beta-oxidation and the degradation of branched amino acids. CONCLUSIONS: The study reported herein significantly expanded our knowledge of the proteome expressed by the oocyst/sporozoite of T. gondii, shedding light on a stage-specifc subset of proteins whose functional profile is consistent with the adaptation of T. gondii oocysts to the nutrient-poor and stressing extracellular environment. FREE ONLINE http://www.biomedcentral.com/1471-2164/14/183
    BMC Genomics 03/2013; 14(1):183. · 4.40 Impact Factor
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    ABSTRACT: Given the lack of knowledge on the rhoptry proteins of Cryptosporidium parvum, we searched for putative members of this protein class in the CryptoDB database using as queries known Toxoplasma gondii rhoptry molecules. We cloned a C. parvum sporozoite cDNA of 4269bp encoding the sushi domain-containing protein cgd8_2530, which shared low amino acid sequence identity, yet a highly conserved domain architecture with the rhoptry neck proteins TgRON1 of T. gondii and PfASP of Plasmodium falciparum. On denaturing and native gels, cgd8_2530 migrated at approximately 150 and 1000 kDa, respectively, suggesting an involvement in a multi-subunit protein complex. Immunoflorescence localised cgd8_2530 to a single, elongated area anterior to sporozoite micronemes and showed protein relocation to the parasite-host cell interface in early epicellular stages. Our data strongly suggest a rhoptry localization for the newly characterised protein, which was therefore renamed C. parvum putative rhoptry protein-1 (CpPRP1).
    Molecular and Biochemical Parasitology 02/2012; 183(1):94-9. · 2.73 Impact Factor
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    ABSTRACT: Among apicomplexan parasites, the coccidia and Cryptosporidium spp. are important pathogens of livestock and humans, and the environmentally resistant stage (oocyst) is essential for their transmission. Little is known of the chemical and molecular composition of the oocyst wall. Currently, the only parasite molecules shown to be involved in oocyst wall formation are the tyrosine-rich proteins gam56, gam82 and gam230 of Eimeria spp. and the cysteine-rich proteins COWP1 and COWP8 of Cryptosporidium parvum. In the present study, we searched the ToxoDB database for the presence of putative Toxoplasma gondii oocyst wall proteins (OWPs) and identified seven candidates, herein named TgOWP1 through TgOWP7, showing homology to the Cryptosporidium COWPs. We analysed a cDNA library from partially sporulated oocysts of T. gondii and cloned the full-length cDNAs encoding TgOWP1, TgOWP2 and TgOWP3, which consist of 499, 462 and 640 amino acids, respectively. The three proteins share 24% sequence identity with each other and a markedly similar overall structure, based on the presence of an N-terminal leader peptide followed by tandem duplications of a six-cysteine amino acid motif closely related to the Type I repeat of COWPs. Using antisera to recombinant TgOWP1, TgOWP2 and TgOWP3, we showed by Western blot that these molecules are expressed in T. gondii oocysts but are not detectable in tachyzoites. The solubilisation of TgOWP1-3 strictly depended on the presence of reducing agents, consistent with a likely involvement of these proteins in multimeric complexes mediated by disulphide bridges. Immunofluorescence analysis allowed the localisation of TgOWP1, TgOWP2 and TgOWP3 to the oocyst wall. Additionally, using immunoelectron microscopy and the 1G12 monoclonal antibody, TgOWP3 was specifically detected in the outer layer of the oocyst wall, thus representing the first validated molecular marker of this structure in T. gondii.
    International journal for parasitology 12/2010; 40(14):1639-49. · 3.39 Impact Factor
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    ABSTRACT: Bioinformatic data show that, in addition to TRAP-C1, Cryptosporidium parvum encodes 11 thrombospondin-related proteins (CpTSP2 through CpTSP12), none of which has been characterized yet. We describe herein the cloning of a 2048 bp-long sporozoite cDNA encoding CpTSP8, a type I integral membrane protein of 614 amino acids, possessing three thrombospondin type I (TSP1) repeats and one epidermal growth factor (EGF)-like domain. Transcriptionally, CpTSP8 is represented by a fully spliced and two immature mRNA forms, in which the intron is either totally or partially retained. Immunofluorescence analysis detected CpTSP8 in the apical complex of both sporozoites and type I merozoites, and showed that, upon sporozoite exposure to host cells in vitro, the protein is translocated onto the parasite surface as typical of micronemal proteins (MICs). Accordingly, double immunofluorescence localized CpTSP8 to C. parvum micronemes, prompting us to rename it CpMIC1 in agreement with the current MICs nomenclature.
    Molecular and Biochemical Parasitology 02/2008; 157(1):98-101. · 2.73 Impact Factor
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    ABSTRACT: We used contour-clamped homogeneous electric field (CHEF) gel electrophoresis and Southern blot hybridization to analyze the molecular karyotype of Cryptosporidium parvum and establish the chromosomal location of 12 single copy genes. In agreement with previous studies, the molecular karyotype of C. parvum was found to consist of partially co-migrating chromosomes ranging in size from 0.97 to 1.55 Mb and segregating into five distinct electrophoretic bands. Hybridization results allowed the definition of a linkage group comprised of five distinct loci located on chromosome VI. Southern hybridization and restriction analysis of total C. parvum chromosomes or isolated chromosome VI using gene-specific probes and an oligonucleotide specific for C. parvum telomeres allowed the development of a long-range restriction map of chromosome VI.
    FEMS Microbiology Letters 01/2006; 175(2):231 - 238. · 2.05 Impact Factor
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    ABSTRACT: Thrombospondin-related adhesive protein of Cryptosporidium 1 (TRAP-C1) belongs to a group of proteins that are also found in Toxoplasma gondii, Eimeria tenella, and Plasmodium species. TRAP-related proteins are needed for gliding motility, host-cell attachment, and invasion. The objective of this study was to characterize the antibody response to recombinant TRAP-C1 (rTRAP-C1) in healthy volunteers exposed to C. parvum and their association with clinical illness. A total of 31 healthy adult volunteers participated. Seven volunteers received the C. parvum TAMU isolate (inocula, 10 to 300 oocysts), and 24 volunteers received the C. parvum UCP isolate (500 to 10(5) oocysts). The total antibody (immunoglobulin M [IgM], IgG, and IgA) response to rTRAP C-1 was measured by enzyme-linked immunosorbent assays prior to and after exposure to Cryptosporidium parvum (days 0 to 45). Results of this study showed that individuals who were uninfected demonstrated higher reactivity at baseline compared to those who became infected. After challenge, increases in antibody reactivity were seen on days 30 and 45 compared to the results seen on days 0 to 5. The increases in antibody reactivity were statistically significant in subjects with diarrhea and with or without detectable oocysts compared to the results seen with those who were uninfected and asymptomatic. These findings suggest that increases in antibody reactivity to rTRAP-C1 occur after recent exposure to C. parvum.
    Clinical and Diagnostic Laboratory Immunology 04/2004; 11(2):235-8. · 2.51 Impact Factor
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    ABSTRACT: We have recently characterised, in the virulent strain RH of Toxoplasma gondii, three glycosylphosphatidylinositol-anchored surface antigens related to SAG1 (p30) and encoded by highly homologous, tandemly arrayed genes named SAG5A, SAG5B and SAG5C. In the present study, we compared the genomic organisation of the SAG5 locus in strains belonging to the three major genotypes of T. gondii. Southern blot analysis using a SAG5-specific probe produced two related but distinct hybridisation patterns, one exclusive of genotype I virulent strains, the other shared by avirulent strains of either genotype II or genotype III. To understand the molecular bases of this intergenotypic heterogeneity, we cloned and sequenced the SAG5 locus in the genotype II strain Me49. We found that in this isolate the SAG5B gene is missing, with SAG5A and SAG5C laying contiguously. This genomic arrangement explains the hybridisation profiles observed for all the avirulent strains examined and indicates that the presence of SAG5B is a distinctive trait of genotype I. Furthermore, we identified two novel SAG1-related genes, SAG5D and SAG5E, mapping respectively 1.8 and 4.0 kb upstream of SAG5A. SAG5D is transcribed in tachyzoites and encodes a polypeptide of 362 amino acids sharing 50% identity with SAG5A-C, whereas SAG5E is a transcribed pseudogene. We also evaluated polymorphisms at the SAG5 locus by comparing the coding regions of SAG5A-E from strains representative of the three archetypal genotypes. In agreement with the strict allelic dimorphism of T. gondii, we identified two alleles for SAG5D, whereas SAG5A, SAG5C and SAG5E were found to be three distinct nucleotide variants. The higher intergenotypic polymorphism of SAG5A, SAG5C and SAG5E suggests that these genes underwent a more rapid genetic drift than the other members of the SAG1 family. Finally, we developed a new PCR-restriction fragment length polymorphism method based on the SAG5C gene that is able to discriminate between strains of genotype I, II and III by a single endonuclease digestion.
    International Journal for Parasitology 01/2004; 33(14):1605-16. · 3.64 Impact Factor
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    ABSTRACT: We have identified three novel Toxoplasma gondii proteins showing close structural similarity to molecules of the SAG1 family, a group of glycosylphosphatidylinositol-anchored surface antigens expressed by the invasive stages of T. gondii. The novel proteins, denominated SAG5A, SAG5B and SAG5C, are encoded by tandemly arrayed and tightly clustered genes containing no introns. The 367 amino acid-long SAG5B and SAG5C are 97.5% identical to each other, whereas SAG5A (362 amino acids) consists of a C-terminal domain sharing 98% identity with SAG5B and SAG5C, and an N-terminal domain whose identity to the other SAG5 polypeptides is only 42%. Expression analysis of the T. gondii strains RH (virulent) and 76 K (avirulent) showed that all members of the SAG5 cluster are transcribed in T. gondii tachyzoites and bradyzoites. However, immunoblot studies on the RH strain revealed that the synthesis of SAG5A does not occur in tachyzoites and is possibly controlled at the post-transcriptional level. On the contrary, SAG5B and SAG5C were detected by immunoblot in tachyzoite lysates and found to migrate in the 40-45 kDa range under reducing conditions or at approximately 34 kDa under unreduced conditions. Triton X-114 partitioning of tachyzoite protein lysates treated with phosphatidylinositol-specific phospholipase C indicated that SAG5B and SAG5C are glycosylphosphatidylinositol-anchored membrane-associated molecules. Consistently, immunofluorescence analysis of transformed tachyzoites over-expressing SAG5B or SAG5C showed that these molecules are targeted to the parasite surface. The characterisation of the SAG5 locus sheds further light on the complex repertoire of SAG1-related genes in T. gondii, that now comprises 14 highly homologous members and five distantly related genes belonging to the SAG2 family.
    International Journal for Parasitology 03/2002; 32(2):121-31. · 3.64 Impact Factor
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    ABSTRACT: We have cloned and sequenced the ribosomal internal transcribed spacer-1 (ITS1) of Cryptosporidium wrairi. Phylogenetic analysis of this region provided further support to the validity of C. wrairi as a distinct species and also to the concept that many of the genotypes recently identified within C. parvum are in fact separate species. Analysis placed the "cattle" and "mouse" genotypes of C. parvum as each other's closest relatives and C. wrairi as a sister group to these two genotypes, followed by the "human" genotype.
    Parassitologia 01/2002; 43(4):159-63.
  • S Cacciò, F Spano, E Pozio
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    ABSTRACT: The genetic polymorphism among 57 Cryptosporidium parvum isolates belonging to genotype 'C' was studied by PCR amplification and the sequencing of two microsatellite loci (ML1 and ML2). A comparative analysis of DNA sequences showed the presence of three (ML1-238, ML1-226, and ML1-220) and seven (ML2-231, ML2-229, ML2-227, ML2-213, ML2-193, ML2-191, and ML2-187) different alleles at these two loci. Alleles differed by expansions/contractions of the microsatellite repeats that generated length polymorphisms. Some alleles were found to be associated with infections of all examined hosts (calf, kid, lamb, and human), whereas others were either associated with a single host, or were geographically restricted. When considering the information from both loci, some preferential associations between alleles are apparent. These data confirm the utility of microsatellite markers for the molecular identification of C. parvum, which is of particular relevance in the investigation of the source of infection of outbreaks and single cases, as well as for genetic studies.
    International Journal for Parasitology 09/2001; 31(10):1082-6. · 3.64 Impact Factor
  • Furio Spano, Andrea Crisanti
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    ABSTRACT: The eukaryotic translation initiation factor eIF-4A is an ATP-dependent RNA helicase involved in ribosome attachment to the 5' end of mRNAs. Employing as a probe a Cryptosporidium parvum genomic amplicon encoding a partial polypeptide related to eIF-4A, we screened a C. parvum sporozoite cDNA library to clone the full length of the gene. Two complete cDNAs were characterized, Cp.F6 and Cp.F10, which consisted of 1,900 and 1,418 bp, respectively. The overlapping portions of the sequences shared 100% identity and encoded a polypeptide of 405 amino acids whose identity to known eIF-4A molecules ranged between 77 and 39%. The 2 cDNAs differed in the length of their respective 3' untranslated regions, of 577 bp in Cp.F6 and 72 bp in Cp.F10, in both of which a putative polyadenylation signal was identified. The structure of the cloned cDNAs, along with genomic Southern blot data indicating that eIF-4A is encoded by a single copy gene, strongly suggested that Cp.F6 and Cp.F10 reflect a differential 3' end processing of mRNA precursors, not observed so far in C. parvum. Northern blot analysis confirmed that the sporozoites express 2 eIF-4A mRNAs and showed that the lower molecular weight transcript is 10- to 20-fold more abundant. We also investigated the polymorphism of the eIF-4A gene and defined a novel polymerase chain reaction-restriction fragment length polymorphism marker discriminating between C. parvum isolates of genotypes 1 and 2.
    Journal of Parasitology 09/2000; 86(4):777-82. · 1.32 Impact Factor
  • Furio Spano, Andrea Crisanti
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    ABSTRACT: The coccidium Cryptosporidium parvum is an obligate intracellular parasite of the phylum Apicomplexa. It infects the gastrointestinal tract of humans and livestock, and represents the third major cause of diarrhoeal disease worldwide. Scarcely considered for decades due to its apparently non-pathogenic nature, C. parvum has been studied very actively over the last 15 years, after its medical relevance as a dangerous opportunistic parasite and widespread water contaminant was fully recognised. Despite the lack of an efficient in vitro culture system and appropriate animal models, significant advances have been made in this relatively short period of time towards understanding C. parvum biology, immunology, genetics and epidemiology. Until recently, very little was known about the genome of C. parvum, with even basic issues, such as the number and size of chromosomes, being the object of a certain controversy. With the advent of pulsed field gradient electrophoresis and the introduction of molecular biology techniques, the overall structure and fine organisation of the genome of C. parvum have started to be disclosed. Organised into eight chromosomes distributed in a very narrow range of molecular masses, the genome of C. parvum is one of the smallest so far described among unicellular eukaryotic organisms. Although fewer than 30 C. parvum genes have been cloned so far, information about the overall structure of the parasite genome has increased exponentially over the last 2 years. From the first karyotypic analyses to the recent development of physical maps for individual chromosomes, this review will try to describe the state-of-the-art of our knowledge on the nuclear genome of C. parvum and will discuss the available experimental evidence concerning the presence of extra-chromosomal elements.
    International Journal for Parasitology 05/2000; · 3.64 Impact Factor
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    ABSTRACT: In this paper the authors question whether the development of a vaccine against cryptosporidiosis could be taken into consideration. The necessity and feasibility of such a vaccine for human and veterinary application is discussed. Developmental stages within the life cycle of the parasite that might act as possible targets for vaccine development are summarised, as well as the target antigens offered by molecular biology and immunology studies. Vaccination trials against cryptosporidiosis carried out so far, including the active and passive immunisation approach, are also overviewed. It seems that with respect to a Cryptosporidium vaccine two target groups can be considered: children of the developing world and neonatal ruminants. Antigens representing possible candidates for a subunit vaccine were identified based on their function, location and/or the immune response they evoke. While the active vaccination of newborn calves, lambs and goat kids has to face a number of important limitations, the passive immunisation approach, where dams were immunised to protect their progeny by colostral transfer, was proven to be a valuable alternative. Finally, a number of points of action for the near future are put forward.
    International Journal for Parasitology 09/1999; 29(8):1289-306. · 3.64 Impact Factor
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    ABSTRACT: We used contour-clamped homogeneous electric field (CHEF) gel electrophoresis and Southern blot hybridization to analyze the molecular karyotype of Cryptosporidium parvum and establish the chromosomal location of 12 single copy genes. In agreement with previous studies, the molecular karyotype of C. parvum was found to consist of partially co-migrating chromosomes ranging in size from 0.97 to 1.55 Mb and segregating into five distinct electrophoretic bands. Hybridization results allowed the definition of a linkage group comprised of five distinct loci located on chromosome VI. Southern hybridization and restriction analysis of total C. parvum chromosomes or isolated chromosome VI using gene-specific probes and an oligonucleotide specific for C. parvum telomeres allowed the development of a long-range restriction map of chromosome VI.
    FEMS Microbiology Letters 07/1999; 175(2):231-8. · 2.05 Impact Factor
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    ABSTRACT: A number of severe diseases of medical and veterinary importance are caused by parasites of the phylum Apicomplexa. These parasites invade host cells using similar subcellular structures, organelles and molecular species. Proteins containing one or more copies of the type I repeat of human platelet thrombospondin (TSP1), are crucial components of both locomotion and invasion machinery. Members of this family have been identified in Eimeria tenella, E. maxima, Toxoplasma gondii, Cryptosporidium parvum and in all Plasmodium species so far analysed. Here, Andrea Crisanti and colleagues discuss the structure, localization and current understanding of the function of TSP family members in the invasion of target cells by apicomplexan parasites.
    Parasitology Today 01/1999; 14(12):479-84. · 5.51 Impact Factor
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    ABSTRACT: The apicomplexan parasite Cryptosporidium parvum invades and multiplies primarily in the brush border cells of the intestinal mucosa causing in AIDS patients a severe diarrhoea that represents a significant contributing factor leading to death. Morphological analysis indicates that the invasion machinery of C. parvum is similar to the apical complex of other parasites of the phylum Apicomplexa. We provide here evidence indicating that C. parvum also shares with these parasites a molecule crucial for the invasion of host cells. We have cloned a 3894 bp-long C. parvum cDNA encoding a protein characterised by sequence and structural similarities with members of the thrombospondin (TSP) family previously described in apicomplexan parasites of the genera Toxoplasma, Eimeria and Plasmodium. This novel C. parvum molecule, the TSP-related adhesive protein of Cryptosporidium-1 (TRAP-C1), is encoded by a single copy gene containing no introns. TRAP-C1 is localised in the apical end of C. parvum sporozoites and is structurally related to the micronemal proteins MIC2 of Toxoplasma and Etp100 of Eimeria, which are involved in host-cell attachment and/or invasion. The identification of TRAP-C1 sheds new light on the molecules possibly involved in the invasion process of intestinal cells by C. parvum. We have also analysed the sequence variation of TRAP-C1 among C. parvum isolates and in the closely related species C. wrairi.
    Molecular and Biochemical Parasitology. 04/1998;
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    ABSTRACT: The apicomplexan parasite Cryptosporidium parvum invades and multiplies primarily in the brush border cells of the intestinal mucosa causing in AIDS patients a severe diarrhoea that represents a significant contributing factor leading to death. Morphological analysis indicates that the invasion machinery of C. parvum is similar to the apical complex of other parasites of the phylum Apicomplexa. We provide here evidence indicating that C. parvum also shares with these parasites a molecule crucial for the invasion of host cells. We have cloned a 3894 bp-long C. parvum cDNA encoding a protein characterised by sequence and structural similarities with members of the thrombospondin (TSP) family previously described in apicomplexan parasites of the genera Toxoplasma, Eimeria and Plasmodium. This novel C. parvum molecule, the TSP-related adhesive protein of Cryptosporidium-1 (TRAP-C1), is encoded by a single copy gene containing no introns. TRAP-C1 is localised in the apical end of C. parvum sporozoites and is structurally related to the micronemal proteins MIC2 of Toxoplasma and Etp100 of Eimeria, which are involved in host-cell attachment and/or invasion. The identification of TRAP-C1 sheds new light on the molecules possibly involved in the invasion process of intestinal cells by C. parvum. We have also analysed the sequence variation of TRAP-C1 among C. parvum isolates and in the closely related species C. wrairi.
    Molecular and Biochemical Parasitology - MOL BIOCHEM PARASITOL. 01/1998; 92(1):147-162.
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    ABSTRACT: Cryptosporidium wrairi was isolated from guinea pigs during a spontaneous outbreak of cryptosporidiosis. Despite the morphological and antigenic similarities to C. parvum, C. wrairi displayed a different host range and site of infection and may represent a separate species or sub-species. We used the polymerase chain reaction to clone two distinct 550 bp-long DNA fragments, Wc-I and Wc-II, of the gene encoding the Cryptosporidium oocyst wall protein (COWP) of C. wrairi, which showed 98% identity to the C. parvum homologue. Within Wc-I, polymorphic RsaI restriction sites were used to develop a polymerase chain reaction-restriction fragment length polymorphism method able to distinguish C. wrairi from C. parvum and to identify two groups of C. parvum isolates differentially associated with animal and human infections.
    FEMS Microbiology Letters 04/1997; 150(2):209 - 217. · 2.05 Impact Factor

Publication Stats

247 Citations
49.67 Total Impact Points

Institutions

  • 2002–2013
    • Istituto Superiore di Sanità
      • Department of Infectious, Parasitic and Immune-mediated Diseases
      Roma, Latium, Italy
    • Murdoch University
      • School of Veterinary and Life Sciences
      Perth, Western Australia, Australia
  • 2008
    • Ospedale Pediatrico Bambino Gesù
      Roma, Latium, Italy
  • 1997–2006
    • Sapienza University of Rome
      Roma, Latium, Italy
    • Imperial College London
      Londinium, England, United Kingdom