Abstract:
:Broadly neutralizing antibodies have been isolated that bind the glycan shield of the HIV-1 envelope spike. One such antibody, PGT135, contacts the intrinsic mannose patch of gp120 at the Asn332, Asn392, and Asn386 glycosylation sites. Here, site-specific glycosylation analysis of recombinant gp120 revealed glycan microheterogeneity sufficient to explain the existence of a minor population of virions resistant to PGT135 neutralization. Target microheterogeneity and antibody glycan specificity are therefore important parameters in HIV-1 vaccine design.
journal_name
J Viroljournal_title
Journal of virologyauthors
Pritchard LK,Spencer DI,Royle L,Vasiljevic S,Krumm SA,Doores KJ,Crispin Mdoi
10.1128/JVI.00230-15subject
Has Abstractpub_date
2015-07-01 00:00:00pages
6952-9issue
13eissn
0022-538Xissn
1098-5514pii
JVI.00230-15journal_volume
89pub_type
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pub_type: 杂志文章
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doi:10.1128/JVI.63.6.2835-2840.1989
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pub_type: 杂志文章
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journal_title:Journal of virology
pub_type: 杂志文章
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abstract::H5N1 and H9N2 avian influenza virus subtypes top the World Health Organization's list for the greatest pandemic potential. Inactivated H5N1 vaccines induce limited immune responses and, in the case of live-attenuated influenza virus vaccines (LAIV), there are safety concerns regarding the possibility of reassortment b...
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pub_type: 杂志文章
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