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VRC34-Antibody Lineage Development Reveals How a Required Rare Mutation Shapes the Maturation of a Broad HIV-Neutralizing Lineage.

Shen CH, DeKosky BJ, Guo Y, Xu K, Gu Y, Kilam D, Ko SH, Kong R, Liu K, Louder MK, Ou L, Zhang B, Chao CW, Corcoran MM, Feng E, Huang J, Normandin E, O'Dell S, Ransier A, Rawi R, Sastry M, Schmidt SD, Wang S, Wang Y, Chuang GY, Doria-Rose NA, Lin B, Zhou T, Boritz EA, Connors M, Douek DC, Karlsson Hedestam GB, Sheng Z, Shapiro L, Mascola JR, Kwong PD
Cell Host Microbe 27 531-543.e6 (2020)
Related entries: 6ubi, 6uce

Cited: 13 times
EuropePMC logo PMID: 32130953

Abstract

Rare mutations have been proposed to restrict the development of broadly neutralizing antibodies against HIV-1, but this has not been explicitly demonstrated. We hypothesized that such rare mutations might be identified by comparing broadly neutralizing and non-broadly neutralizing branches of an antibody-developmental tree. Because sequences of antibodies isolated from the fusion peptide (FP)-targeting VRC34-antibody lineage suggested it might be suitable for such rare mutation analysis, we carried out next-generation sequencing (NGS) on B cell transcripts from donor N123, the source of the VRC34 lineage, and functionally and structurally characterized inferred intermediates along broadly neutralizing and poorly neutralizing developmental branches. The broadly neutralizing VRC34.01 branch required the rare heavy-chain mutation Y33P to bind FP, whereas the early bifurcated VRC34.05 branch did not require this rare mutation and evolved less breadth. Our results demonstrate how a required rare mutation can restrict development and shape the maturation of a broad HIV-1-neutralizing antibody lineage.

Articles - 6ucf mentioned but not cited (2)

  1. VRC34-Antibody Lineage Development Reveals How a Required Rare Mutation Shapes the Maturation of a Broad HIV-Neutralizing Lineage. Shen CH, DeKosky BJ, Guo Y, Xu K, Gu Y, Kilam D, Ko SH, Kong R, Liu K, Louder MK, Ou L, Zhang B, Chao CW, Corcoran MM, Feng E, Huang J, Normandin E, O'Dell S, Ransier A, Rawi R, Sastry M, Schmidt SD, Wang S, Wang Y, Chuang GY, Doria-Rose NA, Lin B, Zhou T, Boritz EA, Connors M, Douek DC, Karlsson Hedestam GB, Sheng Z, Shapiro L, Mascola JR, Kwong PD. Cell Host Microbe 27 531-543.e6 (2020)
  2. Crystal structures of the human IgD Fab reveal insights into CH1 domain diversity. Davies AM, Beavil RL, Barbolov M, Sandhar BS, Gould HJ, Beavil AJ, Sutton BJ, McDonnell JM. Mol Immunol 159 28-37 (2023)


Reviews citing this publication (3)

  1. Neutralizing Antibodies Targeting HIV-1 gp41. Caillat C, Guilligay D, Sulbaran G, Weissenhorn W. Viruses 12 E1210 (2020)
  2. Advancing HIV Broadly Neutralizing Antibodies: From Discovery to the Clinic. Spencer DA, Shapiro MB, Haigwood NL, Hessell AJ. Front Public Health 9 690017 (2021)
  3. Strategies for HIV-1 vaccines that induce broadly neutralizing antibodies. Haynes BF, Wiehe K, Borrrow P, Saunders KO, Korber B, Wagh K, McMichael AJ, Kelsoe G, Hahn BH, Alt F, Shaw GM. Nat Rev Immunol (2022)

Articles citing this publication (8)

  1. Broadly neutralizing antibodies target the coronavirus fusion peptide. Dacon C, Tucker C, Peng L, Lee CD, Lin TH, Yuan M, Cong Y, Wang L, Purser L, Williams JK, Pyo CW, Kosik I, Hu Z, Zhao M, Mohan D, Cooper AJR, Peterson M, Skinner J, Dixit S, Kollins E, Huzella L, Perry D, Byrum R, Lembirik S, Drawbaugh D, Eaton B, Zhang Y, Yang ES, Chen M, Leung K, Weinberg RS, Pegu A, Geraghty DE, Davidson E, Douagi I, Moir S, Yewdell JW, Schmaljohn C, Crompton PD, Holbrook MR, Nemazee D, Mascola JR, Wilson IA, Tan J. Science 377 728-735 (2022)
  2. Development of Martini 2.2 parameters for N-glycans: a case study of the HIV-1 Env glycoprotein dynamics. Chakraborty S, Wagh K, Gnanakaran S, López CA. Glycobiology 31 787-799 (2021)
  3. Development of Neutralization Breadth against Diverse HIV-1 by Increasing Ab-Ag Interface on V2. Gao N, Gai Y, Meng L, Wang C, Wang W, Li X, Gu T, Louder MK, Doria-Rose NA, Wiehe K, Nazzari AF, Olia AS, Gorman J, Rawi R, Wu W, Smith C, Khant H, de Val N, Yu B, Luo J, Niu H, Tsybovsky Y, Liao H, Kepler TB, Kwong PD, Mascola JR, Qin C, Zhou T, Yu X, Gao F. Adv Sci (Weinh) 9 e2200063 (2022)
  4. Highly protective antimalarial antibodies via precision library generation and yeast display screening. Banach BB, Tripathi P, Da Silva Pereira L, Gorman J, Nguyen TD, Dillon M, Fahad AS, Kiyuka PK, Madan B, Wolfe JR, Bonilla B, Flynn B, Francica JR, Hurlburt NK, Kisalu NK, Liu T, Ou L, Rawi R, Schön A, Shen CH, Teng IT, Zhang B, Pancera M, Idris AH, Seder RA, Kwong PD, DeKosky BJ. J Exp Med 219 e20220323 (2022)
  5. Rapid selection of HIV envelopes that bind to neutralizing antibody B cell lineage members with functional improbable mutations. Swanson O, Rhodes B, Wang A, Xia SM, Parks R, Chen H, Sanzone A, Cooper M, Louder MK, Lin BC, Doria-Rose NA, Bonsignori M, Saunders KO, Wiehe K, Haynes BF, Azoitei ML. Cell Rep 36 109561 (2021)
  6. Antibody-directed evolution reveals a mechanism for enhanced neutralization at the HIV-1 fusion peptide site. Banach BB, Pletnev S, Olia AS, Xu K, Zhang B, Rawi R, Bylund T, Doria-Rose NA, Nguyen TD, Fahad AS, Lee M, Lin BC, Liu T, Louder MK, Madan B, McKee K, O'Dell S, Sastry M, Schön A, Bui N, Shen CH, Wolfe JR, Chuang GY, Mascola JR, Kwong PD, DeKosky BJ. Nat Commun 14 7593 (2023)
  7. Dependence on a variable residue limits the breadth of an HIV MPER neutralizing antibody, despite convergent evolution with broadly neutralizing antibodies. Scheepers C, Kgagudi P, Mzindle N, Gray ES, Moyo-Gwete T, Lambson BE, Oosthuysen B, Mabvakure B, Garrett NJ, Abdool Karim SS, Morris L, Moore PL. PLoS Pathog 18 e1010450 (2022)
  8. Epitope-focused immunogen design based on the ebolavirus glycoprotein HR2-MPER region. Schoeder CT, Gilchuk P, Sangha AK, Ledwitch KV, Malherbe DC, Zhang X, Binshtein E, Williamson LE, Martina CE, Dong J, Armstrong E, Sutton R, Nargi R, Rodriguez J, Kuzmina N, Fiala B, King NP, Bukreyev A, Crowe JE, Meiler J. PLoS Pathog 18 e1010518 (2022)


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