Mapping the complete glycoproteome of virion-derived HIV-1 gp120 provides insights into broadly neutralizing antibody binding-Reference-Cited by-同舟云学术

Mapping the complete glycoproteome of virion-derived HIV-1 gp120 provides insights into broadly neutralizing antibody binding

Published:2016-09-08 Issue:1 Volume:6 Page:
ISSN:2045-2322
Container-title:Scientific Reports
language:en
Short-container-title:Sci Rep

Author:

Panico Maria,Bouché Laura,Binet Daniel,O’Connor Michael-John,Rahman Dinah,Pang Poh-Choo,Canis Kevin,North Simon J.,Desrosiers Ronald C.,Chertova Elena,Keele Brandon F.,Bess Julian W.,Lifson Jeffrey D.,Haslam Stuart M.,Dell Anne,Morris Howard R.

Publisher

Springer Science and Business Media LLC

Subject

Multidisciplinary

Link

http://www.nature.com/articles/srep32956.pdf

Reference52 articles.

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2. Qi, Y., Jo, S. & Im, W. Roles of glycans in interactions between gp120 and HIV broadly neutralizing antibodies. Glycobiology 26, 251–260, doi: 10.1093/glycob/cwv101 (2016).

3. Mizuochi, T. et al. Carbohydrate structures of the human-immunodeficiency-virus (HIV) recombinant envelope glycoprotein gp120 produced in Chinese-hamster ovary cells. Biochem J 254, 599–603 (1988).

4. Zhu, X., Borchers, C., Bienstock, R. J. & Tomer, K. B. Mass spectrometric characterization of the glycosylation pattern of HIV-gp120 expressed in CHO cells. Biochemistry 39, 11194–11204 (2000).

5. Go, E. P. et al. Glycosylation site-specific analysis of clade C HIV-1 envelope proteins. Journal of proteome research 8, 4231–4242, doi: 10.1021/pr9002728 (2009).

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