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TitleDiscovery, recognized antigenic structures, and evolution of cross-serotype broadly neutralizing antibodies from porcine B-cell repertoires against foot-and-mouth disease virus.
Journal, issue, pagesPLoS Pathog, Vol. 20, Issue 10, Page e1012623, Year 2024
Publish dateOct 15, 2024
AuthorsFengjuan Li / Shanquan Wu / Lv Lv / Shulun Huang / Zelin Zhang / Zhaxi Zerang / Pinghua Li / Yimei Cao / Huifang Bao / Pu Sun / Xingwen Bai / Yong He / Yuanfang Fu / Hong Yuan / Xueqing Ma / Zhixun Zhao / Jing Zhang / Jian Wang / Tao Wang / Dong Li / Qiang Zhang / Jijun He / Zaixin Liu / Zengjun Lu / Dongsheng Lei / Kun Li /
PubMed AbstractIt is a great challenge to isolate the broadly neutralizing antibodies (bnAbs) against foot-and-mouth disease virus (FMDV) due to its existence as seven distinct serotypes without cross-protection. ...It is a great challenge to isolate the broadly neutralizing antibodies (bnAbs) against foot-and-mouth disease virus (FMDV) due to its existence as seven distinct serotypes without cross-protection. Here, by vaccination of pig with FMDV serotypes O and A whole virus antigens, we obtained 10 bnAbs against serotypes O, A and/or Asia1 by dissecting 216 common clonotypes of two serotypes O and A specific porcine B-cell receptor (BCR) gene repertoires containing total 12720 B cell clones, indicating the induction of cross-serotype bnAbs after sequential vaccination with serotypes O and A antigens. The majority of porcine bnAbs (9/10) were derived from terminally differentiated B cells of different clonal lineages, which convergently targeted the conserved "RGDL" motif on structural protein VP1 of FMDV by mimicking receptor recognition to inhibit viral attachment to cells. Cryo-EM complex structures revealed that the other bnAb pOA-2 specifically targets a novel inter-pentamer antigen structure surrounding the viral three-fold axis, with a highly conserved determinant at residue 68 on VP2. This unique binding pattern enabled cross-serotype neutralization by destabilizing the viral particle. The evolutionary analysis of pOA-2 demonstrated its origin from an intermediate B-cell, emphasizing the crucial role of somatic hypermutations (SHMs) in balancing the breadth and potency of neutralization. However, excessive SHMs may deviate from the trajectory of broad neutralization. This study provides a strategy to uncover bnAbs against highly mutable pathogens and the cross-serotype antigenic structures to explore broadly protective FMDV vaccine.
External linksPLoS Pathog / PubMed:39405339 / PubMed Central
MethodsEM (single particle)
Resolution2.44 - 2.52 Å
Structure data

38814

8y0q

EMDB-38814, PDB-8y0q:
Complex of FMDV O/18074 and inter-serotype broadly neutralizing antibodies pOA-2
Method: EM (single particle) / Resolution: 2.44 Å

38815

8y0r

EMDB-38815, PDB-8y0r:
Complex of FMDV A/WH/CHA/09 and inter-serotype broadly neutralizing antibodies pOA-2
Method: EM (single particle) / Resolution: 2.52 Å

Source
  • foot-and-mouth disease virus o
  • sus scrofa (pig)
  • foot-and-mouth disease virus a
KeywordsVIRUS/IMMUNE SYSTEM / Foot-and-mouth disease virus O / Sus scrofa / VIRUS-IMMUNE SYSTEM complex / Foot-and-mouth disease virus A

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