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TitleRecognition determinants of improved HIV-1 neutralization by a heavy chain matured pediatric antibody.
Journal, issue, pagesiScience, Vol. 26, Issue 9, Page 107579, Year 2023
Publish dateSep 15, 2023
AuthorsSanjeev Kumar / Swarandeep Singh / Arnab Chatterjee / Prashant Bajpai / Shaifali Sharma / Sanket Katpara / Rakesh Lodha / Somnath Dutta / Kalpana Luthra /
PubMed AbstractThe structural and characteristic features of HIV-1 broadly neutralizing antibodies (bnAbs) from chronically infected pediatric donors are currently unknown. Herein, we characterized a heavy chain ...The structural and characteristic features of HIV-1 broadly neutralizing antibodies (bnAbs) from chronically infected pediatric donors are currently unknown. Herein, we characterized a heavy chain matured HIV-1 bnAb 44m, identified from a pediatric elite-neutralizer. Interestingly, in comparison to its wild-type AIIMS-P01 bnAb, 44m exhibited moderately higher level of somatic hypermutations of 15.2%. The 44m neutralized 79% of HIV-1 heterologous viruses (n = 58) tested, with a geometric mean IC titer of 0.36 μg/mL. The cryo-EM structure of 44m Fab in complex with fully cleaved glycosylated native-like BG505.SOSIP.664.T332N gp140 envelope trimer at 4.4 Å resolution revealed that 44m targets the V3-glycan N332-supersite and GDIR motif to neutralize HIV-1 with improved potency and breadth, plausibly attributed by a matured heavy chain as compared to that of wild-type AIIMS-P01. This study further improves our understanding on pediatric HIV-1 bnAbs and structural basis of broad HIV-1 neutralization by 44m may be useful blueprint for vaccine design in future.
External linksiScience / PubMed:37649696 / PubMed Central
MethodsEM (single particle)
Resolution4.4 Å
Structure data

EMDB-36815: Recognition determinants of broad and potent HIV-1 neutralization by an affinity matured antibody from a pediatric elite-neutralizer
Method: EM (single particle) / Resolution: 4.4 Å

Source
  • HIV-1 06TG.HT032 (virus)
  • Homo sapiens (human)

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