Article
Enhanced immune responses of mice inoculated recombinant adenoviruses expressing GP5 by fusion with GP3 and/or GP4 of PRRS virus.
Key Laboratory of Animal Diseases Diagnostic and Immunology, College of Veterinary Medicine, Nanjing Agricultural University, Ministry of Agriculture, Nanjing 210095, China.
Virus Research (impact factor:
2.94).
10/2008;
136(1-2):50-7.
DOI:10.1016/j.virusres.2008.04.016
Source: PubMed
-
Citations (0)
- Cited In (2)
-
Article: Immunogenic and protective properties of GP5 and M structural proteins of porcine reproductive and respiratory syndrome virus expressed from replicating but nondisseminating adenovectors.
[show abstract] [hide abstract]
ABSTRACT: Porcine reproductive and respiratory syndrome virus (PRRSV) is responsible for significant economic losses in the porcine industry. Currently available commercial vaccines do not allow optimal and safe protection. In this study, replicating but nondisseminating adenovectors (rAdV) were used for the first time in pigs for vaccinal purposes. They were expressing the PRRSV matrix M protein in fusion with either the envelope GP5 wild-type protein (M-GP5) which carries the major neutralizing antibody (NAb)-inducing epitope or a mutant form of GP5 (M-GP5m) developed to theoretically increase the NAb immune response. Three groups of fourteen piglets were immunized both intramuscularly and intranasally at 3-week intervals with rAdV expressing the green fluorescent protein (GFP, used as a negative control), M-GP5 or M-GP5m. Two additional groups of pigs were primed with M-GP5m-expressing rAdV followed by a boost with bacterially-expressed recombinant wild-type GP5 or were immunized twice with a PRRSV inactivated commercial vaccine. The results show that the rAdV expressing the fusion proteins of interest induced systemic and mucosal PRRSV GP5-specific antibody response as determined in an ELISA. Moreover the prime with M-GP5m-expressing rAdV and boost with recombinant GP5 showed the highest antibody response against GP5. Following PRRSV experimental challenge, pigs immunized twice with rAdV expressing either M-GP5 or M-GP5m developed partial protection as shown by a decrease in viremia overtime. The lowest viremia levels and/or percentages of macroscopic lung lesions were obtained in pigs immunized twice with either the rAdV expressing M-GP5m or the PRRSV inactivated commercial vaccine.Veterinary Research 03/2013; 44(1):17. · 4.06 Impact Factor -
Article: Immune evasion of porcine reproductive and respiratory syndrome virus through glycan shielding involves both glycoprotein 5 as well as glycoprotein 3.
[show abstract] [hide abstract]
ABSTRACT: Passive administration of porcine reproductive and respiratory syndrome virus (PRRSV) neutralizing antibodies (NAbs) can effectively protect pigs against PRRSV infection. However, after PRRSV infection, pigs typically develop a weak and deferred NAb response. One major reason for such a meager NAb response is the phenomenon of glycan shielding involving GP5, a major glycoprotein carrying one major neutralizing epitope. We describe here a type II PRRSV field isolate (PRRSV-01) that is highly susceptible to neutralization and induces an atypically rapid, robust NAb response in vivo. Sequence analysis shows that PRRSV-01 lacks two N-glycosylation sites, normally present in wild-type (wt) PRRSV strains, in two of its envelope glycoproteins, one in GP3 (position 131) and the other in GP5 (position 51). To determine the influence of these missing N-glycosylation sites on the distinct neutralization phenotype of PRRSV-01, a chimeric virus (FL01) was generated by replacing the structural genes of type II PRRSV strain FL12 cDNA infectious clone with those from PRRSV-01. N-glycosylation sites were reintroduced into GP3 and GP5 of FL01, separately or in combination, by site-directed mutagenesis. Reintroduction of the N-glycosylation site in either GP3 or GP5 allowed recovery of in vivo and in vitro glycan shielding capacity, with an additive effect when these sites were reintroduced into both glycoproteins simultaneously. Although the loss of these glycosylation sites has seemingly occurred naturally (presumably by passage through cell cultures), PRRSV-01 virus quickly regains these glycosylation sites through replication in vivo, suggesting that a strong selective pressure is exerted at these sites. Collectively, our data demonstrate the involvement of an N-glycan moiety located in GP3 in glycan shield interference.Journal of Virology 03/2011; 85(11):5555-64. · 5.40 Impact Factor
Data provided are for informational purposes only. Although carefully collected, accuracy cannot be guaranteed.
The impact factor represents a rough estimation of the journal's impact factor and does not reflect the actual
current impact factor.
Publisher conditions are provided by RoMEO. Differing provisions from the publisher's actual policy or licence
agreement may be applicable.
Keywords
2 weeks post-boost-immunization
anti-PRRSV CTL responses
cellular immune response
current vaccination strategies
fusion protein GP3-GP5
fusion proteins GP3-GP5
GP5 protein
higher titers
mouse model
Porcine reproductive
potential vaccine
PRRSV
PRRSV infection
PRRSV-specific antibodies
rAd-GP3-GP5
recombinant adenoviruses rAd-GP3-GP5
replication-defective adenovirus recombinants
respiratory syndrome
stronger lymphocyte proliferation responses
swine industry