สืบค้นงานวิจัย
Glycans flanking the hypervariable connecting peptide between the a and B strands of the V1/V2 domain of HIV-1 gp120 confer resistance to antibodies that neutralize CRF01-AE viruses
O'Rourke S.M. - ไม่ระบุหน่วยงาน
ชื่อเรื่อง (EN): Glycans flanking the hypervariable connecting peptide between the a and B strands of the V1/V2 domain of HIV-1 gp120 confer resistance to antibodies that neutralize CRF01-AE viruses
ผู้แต่ง / หัวหน้าโครงการ (EN): O'Rourke S.M.
บทคัดย่อ (EN): Understanding the molecular determinants of sensitivity and resistance to neutralizing antibodies is critical for the development of vaccines designed to prevent HIV infection. In this study, we used a genetic approach to characterize naturally occurring polymorphisms in the HIV envelope protein that conferred neutralization sensitivity or resistance. Libraries of closely related envelope genes, derived from virus quasi-species, were constructed from individuals infected with CRF01-AE viruses. The libraries were screened with plasma containing broadly neutralizing antibodies, and neutralization sensitive and resistant variants were selected for sequence analysis. In vitro mutagenesis allowed us to identify single amino acid changes in three individuals that conferred resistance to neutralization by these antibodies. All three mutations created N-linked glycosylation sites (two at N136 and one at N149) proximal to the hypervariable connecting peptide between the C-terminus of the A strand and the N-terminus of the B strand in the four-stranded V1/V2 domain β-sheet structure. Although N136 has previously been implicated in the binding of broadly neutralizing monoclonal antibodies, this glycosylation site appears to inhibit the binding of neutralizing antibodies in plasma from HIV-1 infected subjects. Previous studies have reported that the length of the V1/V2 domain in transmitted founder viruses is shorter and possesses fewer glycosylation sites compared to viruses isolated from chronic infections. Our results suggest that vaccine immunogens based on recombinant envelope proteins from clade CRF01-AE viruses might be improved by inclusion of envelope proteins that lack these glycosylation sites. This strategy might improve the efficacy of the vaccines used in the partially © 2015 O'Rourke et al.
บทคัดย่อ: ไม่พบข้อมูลจากหน่วยงานต้นทาง
ภาษา (EN): en
เอกสารแนบ (EN): https://www.scopus.com/inward/record.uri?eid=2-s2.0-84925967803&doi=10.1371%2fjournal.pone.0119608&partnerID=40&md5=d6516edcd20280cce7853431430d9063
เผยแพร่โดย (EN): มหาวิทยาลัยมหิดล
คำสำคัญ (EN): Sequence Alignment
เจ้าของลิขสิทธิ์ (EN): มหาวิทยาลัยมหิดล
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O'Rourke S.M.. "Glycans flanking the hypervariable connecting peptide between the a and B strands of the V1/V2 domain of HIV-1 gp120 confer resistance to antibodies that neutralize CRF01-AE viruses". ไม่ระบุหน่วยงาน. ม.ป.ป.

O'Rourke S.M.. "Glycans flanking the hypervariable connecting peptide between the a and B strands of the V1/V2 domain of HIV-1 gp120 confer resistance to antibodies that neutralize CRF01-AE viruses". ไม่ระบุหน่วยงาน. ม.ป.ป.. Print.



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Glycans flanking the hypervariable connecting peptide between the a and B strands of the V1/V2 domain of HIV-1 gp120 confer resistance to antibodies that neutralize CRF01-AE viruses
O'Rourke S.M.
มหาวิทยาลัยมหิดล
ไม่ระบุวันที่เผยแพร่
Cryptic determinant of a4b7 binding in the v2 loop of hiv-1 gp120 Naturally Occurring Mutations in HIV-1 CRF01_AE Capsid Affect Viral Sensitivity to Restriction Factors HIV-1- specific IgA monoclonal antibodies from an HIV-1 vaccinee mediate galactosylceramide blocking and phagocytosis Identification of new regions in HIV-1 gp120 Variable 2 and 3 Loops that Bind to α4β7 Integrin Receptor National Survey of Pretreatment HIV-Drug Resistance in Thai HIV-1-Infected Adults Optimization of genotyping by phenotypic analysis of clinical HIV-1 subtype CRF01_AE isolates from South-East Asia Prevalence of primary HIV drug resistance in Thailand detected by short reverse transcriptase genotypic resistance assay Characterization of HIV-1 gp120 antibody specificities induced in anogenital secretions of RV144 vaccine recipients after late boost immunizations External Quality Assessment Scheme for HIV-1 Drug Resistance Genotyping in Thailand Monoclonal antibodies, derived from humans vaccinated with the RV144 HIV vaccine containing the HVEM binding domain of herpes simplex virus (HSV) glycoprotein D, neutralize HSV infection, mediate anti
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