Influence of porcine reproductive and respiratory syndrome virus GP5 glycoprotein N-linked glycans on immune responses in mice

التفاصيل البيبلوغرافية
العنوان: Influence of porcine reproductive and respiratory syndrome virus GP5 glycoprotein N-linked glycans on immune responses in mice
المؤلفون: Ping Jiang, Wenming Jiang, Xianwei Wang, Xinglong Wang, Yufeng Li, Yijun Du
المصدر: Virus Genes. 35:663-671
بيانات النشر: Springer Science and Business Media LLC, 2007.
سنة النشر: 2007
مصطلحات موضوعية: Glycosylation, T-Lymphocytes, viruses, Genetic Vectors, Lymphocyte proliferation, Antibodies, Viral, Virus, Adenoviridae, Mice, Immune system, Viral Envelope Proteins, Neutralization Tests, Polysaccharides, Virology, Genetics, Animals, Porcine respiratory and reproductive syndrome virus, Neutralizing antibody, Molecular Biology, Cell Proliferation, Mice, Inbred BALB C, Vaccines, Synthetic, biology, Immunogenicity, Wild type, General Medicine, Porcine reproductive and respiratory syndrome virus, biology.organism_classification, biology.protein, Female, Mutant Proteins, Antibody
الوصف: Porcine reproductive and respiratory syndrome virus (PRRSV) is one of the most economically significant viral diseases in the swine industry. Infection with PRRSV following vaccination is common, since protection is incomplete. Persistent infection may be one of the biggest obstacles to control of the disease. "Glycan shielding" was postulated to be a primary mechanism to explain evasion from neutralizing immune response, ensuring in vivo persistence of virus, such as HIV, SIV, and HBV. The objective of this study was to construct recombinant adenoviruses expressing single or multiple N-linked glycosylation site (NGS) mutant GP5 of PRRSV, and evaluate the expression in cell culture, and potential to induce immune responses in BALB/c mice. Six recombinant adenoviruses were constructed each expressing wild-type GP5 and 1-4 NGS mutants: N44S, N44/51S, N30/44/51S, N30/33/44/51S and N30/33S. Inoculation of BALB/c mice with all five recombinants expressing NGS mutant GP5 resulted in a significant neutralizing antibody responses which were significantly higher than that of recombinant adenovirus expressing wild-type GP5. But there were no significant difference in lymphocyte proliferation responses induced by wild type and NGS mutant GP5. It indicated that glycosylations of GP5 at residues N30, N33, N44 and N51 are critical for induction of neutralizing antibodies. These NGS mutant PRRSV GP5 will be useful to characterize the effects of glycosylation on immunogenicity in the natural host, and may lead to a new approach for the generation of PRRSV vaccines.
تدمد: 1572-994X
0920-8569
الوصول الحر: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d57c2f1236954982a296a55f96f11804Test
https://doi.org/10.1007/s11262-007-0131-yTest
حقوق: CLOSED
رقم الانضمام: edsair.doi.dedup.....d57c2f1236954982a296a55f96f11804
قاعدة البيانات: OpenAIRE