Oligomannose Glycopeptide Conjugates Elicit Antibodies Targeting the Glycan Core Rather than Its Extremities

Nguyen, Dung N.; Xu, Bokai; Stanfield, Robyn L.; Bailey, Jennifer K.; Horiya, Satoru; Temme, J. Sebastian; Leon, Deborah R.; LaBranche, Celia C.; Montefiori, David C.; Costello, Catherine E.; Wilson, Ian A.; Krauss, Isaac J.

doi:10.1021/acscentsci.8b00588

Title: Oligomannose Glycopeptide Conjugates Elicit Antibodies Targeting the Glycan Core Rather than Its Extremities

Journal Article · Wed Feb 06 00:00:00 EST 2019 · ACS Central Science

DOI:https://doi.org/10.1021/acscentsci.8b00588· OSTI ID:1493660

Nguyen, Dung N. ^[1]; Xu, Bokai ^[1]; Stanfield, Robyn L. ^[2]; Bailey, Jennifer K. ^[1]; Horiya, Satoru ^[1]; Temme, J. Sebastian ^[1]; Leon, Deborah R. ^[3]; LaBranche, Celia C. ^[4]; Montefiori, David C. ^[4];

^[3]; Wilson, Ian A. ^[2];

^[1]

Department of Chemistry, Brandeis University, Waltham, Massachusetts 02454-9110, United States
Department of Integrative Structural and Computational Biology and the Skaggs Institute for Chemical Biology, The Scripps Research Institute, La Jolla, California 92037, United States
Department of Biochemistry, Center for Biomedical Mass Spectrometry, Boston University School of Medicine, Boston, Massachusetts 02215, United States
Department of Surgery, Duke University Medical Center, Durham, North Carolina 27710, United States

Up to ~20% of HIV-infected individuals eventually develop broadly neutralizing antibodies (bnAbs), and many of these antibodies (~40%) target a region of dense high-mannose glycosylation on gp120 of the HIV envelope protein, known as the “high-mannose patch” (HMP). Thus, there have been numerous attempts to develop glycoconjugate vaccine immunogens that structurally mimic the HMP and might elicit bnAbs targeting this conserved neutralization epitope. Herein, we report on the immunogenicity of glycopeptides, designed by in vitro selection, that bind tightly to anti-HMP antibody 2G12. By analyzing the fine carbohydrate specificity of rabbit antibodies elicited by these immunogens, we found that they differ from some natural human bnAbs, such as 2G12 and PGT128, in that they bind primarily to the core structures within the glycan, rather than to the Manα1 → 2Man termini (2G12) or to the whole glycan (PGT128). Antibody specificity for the glycan core may result from extensive serum mannosidase trimming of the immunogen in the vaccinated animals. This finding has broad implications for vaccine design aiming to target glycan-dependent HIV neutralizing antibodies.

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Research Organization:: SLAC National Accelerator Lab., Menlo Park, CA (United States)

Sponsoring Organization:: USDOE Office of Science (SC), Basic Energy Sciences (BES); National Inst. of Health; USDOE Office of Science (SC), Biological and Environmental Research (BER)

Grant/Contract Number:: AC02-76SF00515; HHSN27201100016C; P41GM103393

OSTI ID:: 1493660

Alternate ID(s):: OSTI ID: 1508820

Journal Information:: ACS Central Science, Journal Name: ACS Central Science Vol. 5 Journal Issue: 2; ISSN 2374-7943

Publisher:: American Chemical SocietyCopyright Statement

Country of Publication:: United States

Language:: English

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