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Structure and immune recognition of trimeric pre-fusion HIV-1 Env.

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dc.contributor.authorPancera, Marie.
dc.contributor.authorZhou, Tongqing.
dc.contributor.authorDruz, Aliaksandr.
dc.contributor.authorGeorgiev, Ivelin S.
dc.contributor.authorSoto, Cinque.
dc.contributor.authorGorman, Jason.
dc.contributor.authorHuang, Jinghe.
dc.contributor.authorAcharya, Priyamvada.
dc.contributor.authorChuang, Gwo-Yu.
dc.contributor.authorOfek, Gilad.
dc.contributor.authorStewart-Jones, Guillaume B. E.
dc.contributor.authorStuckey, Jonathan.
dc.contributor.authorBailer, Robert T.
dc.contributor.authorJoyce, M. Gordon.
dc.contributor.authorLouder, Mark K.
dc.contributor.authorTumba, Nancy Lola.
dc.contributor.authorYang, Yongping.
dc.contributor.authorZhang, Baoshan.
dc.contributor.authorCohen, Myron S.
dc.contributor.authorHaynes, Barton F.
dc.contributor.authorMascola, John R.
dc.contributor.authorMorris, Lynn.
dc.contributor.authorMunro, James B.
dc.contributor.authorBlanchard, Scott C.
dc.contributor.authorMothes, Walther.
dc.contributor.authorConnors, Mark.
dc.contributor.authorKwong, Peter D.
dc.date.accessioned2016-11-08T09:58:01Z
dc.date.available2016-11-08T09:58:01Z
dc.date.created2014
dc.date.issued2014
dc.descriptionCAPRISA, 2014.en_US
dc.description.abstractThe human immunodeficiency virus type 1 (HIV-1) envelope (Env) spike, comprising three gp120 and three gp41 subunits, is a conformational machine that facilitates HIV-1 entry by rearranging from a mature unliganded state, through receptor-bound intermediates, to a post-fusion state. As the sole viral antigen on the HIV-1 virion surface, Env is both the target of neutralizing antibodies and a focus of vaccine efforts. Here we report the structure at 3.5 Å resolution for an HIV-1 Env trimer captured in a mature closed state by antibodies PGT122 and 35O22. This structure reveals the pre-fusion conformation of gp41, indicates rearrangements needed for fusion activation, and defines parameters of immune evasion and immune recognition. Pre-fusion gp41 encircles amino- and carboxy-terminal strands of gp120 with four helices that form a membrane-proximal collar, fastened by insertion of a fusion peptide-proximal methionine into a gp41-tryptophan clasp. Spike rearrangements required for entry involve opening the clasp and expelling the termini. N-linked glycosylation and sequence-variable regions cover the pre-fusion closed spike; we used chronic cohorts to map the prevalence and location of effective HIV-1-neutralizing responses, which were distinguished by their recognition of N-linked glycan and tolerance for epitope-sequence variation.en_US
dc.identifier.citationPancera, M., Zhou, T., Druz, A., Georgiev, I.S., Soto, C., Gorman, J., Huang, J., Acharya, P., Chuang, G.Y., Ofek, G. and Stewart-Jones, G.B.E., Stuckey, J., Bailer, R.T., Joyce, M.G., Louder, M.K., Tumba, N., Yang, Y., Zhang, B., Cohen, M.S., Barton F. Haynes, B.F., Mascola, J.R., Morris, L., Munro, J.B., Blanchard, S.C., Mothes, W., Connors, M.and Kwong, P.D. 2014. Structure and immune recognition of trimeric pre-fusion HIV-1 Env. Nature 514(7523), 455-461.en_US
dc.identifier.urihttp://dx.doi.org/10.1038/nature13808en_US
dc.identifier.urihttp://hdl.handle.net/10413/13619
dc.language.isoenen_US
dc.publisherMacmillan Publishers Limited.en_US
dc.subjectAIDS Vaccines/chemistry.en_US
dc.subjectAIDS Vaccines/immunology.en_US
dc.subjectAmino Acid Sequence.en_US
dc.subjectCohort Studies.en_US
dc.subjectCrystallography, X-Ray.en_US
dc.subjectGenetic Variation.en_US
dc.subjectGlycosylation.en_US
dc.titleStructure and immune recognition of trimeric pre-fusion HIV-1 Env.en_US
dc.typePeer reviewed journal articleen_US

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