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TitleSARS-CoV-2 hijacks neutralizing dimeric IgA for nasal infection and injury in Syrian hamsters.
Journal, issue, pagesEmerg Microbes Infect, Vol. 12, Issue 2, Page 2245921, Year 2023
Publish dateAug 23, 2023
AuthorsBiao Zhou / Runhong Zhou / Jasper Fuk-Woo Chan / Jianwei Zeng / Qi Zhang / Shuofeng Yuan / Li Liu / Rémy Robinot / Sisi Shan / Na Liu / Jiwan Ge / Hugo Yat-Hei Kwong / Dongyan Zhou / Haoran Xu / Chris Chung-Sing Chan / Vincent Kwok-Man Poon / Hin Chu / Ming Yue / Ka-Yi Kwan / Chun-Yin Chan / Chris Chun-Yiu Chan / Kenn Ka-Heng Chik / Zhenglong Du / Ka-Kit Au / Haode Huang / Hiu-On Man / Jianli Cao / Cun Li / Ziyi Wang / Jie Zhou / Youqiang Song / Man-Lung Yeung / Kelvin Kai-Wang To / David D Ho / Lisa A Chakrabarti / Xinquan Wang / Linqi Zhang / Kwok-Yung Yuen / Zhiwei Chen /
PubMed AbstractPrevention of robust severe acute respiratory syndrome coronavirus-2 (SARS-CoV-2) infection in nasal turbinate (NT) requires evaluation of IgA neutralizing antibodies. Here, we report the efficacy ...Prevention of robust severe acute respiratory syndrome coronavirus-2 (SARS-CoV-2) infection in nasal turbinate (NT) requires evaluation of IgA neutralizing antibodies. Here, we report the efficacy of receptor binding domain (RBD)-specific monomeric B8-mIgA1 and B8-mIgA2, and dimeric B8-dIgA1, B8-dIgA2 and TH335-dIgA1 against intranasal SARS-CoV-2 challenge in Syrian hamsters. These antibodies exhibited comparable neutralization potency against authentic virus by competing with human angiotensin converting enzyme-2 (ACE2) receptor for RBD binding. While reducing viral loads in lungs significantly, prophylactic intranasal B8-dIgA unexpectedly led to high amount of infectious viruses and extended damage in NT compared to controls. Mechanistically, B8-dIgA failed to inhibit SARS-CoV-2 cell-to-cell transmission, but was hijacked by the virus through dendritic cell-mediated trans-infection of NT epithelia leading to robust nasal infection. Cryo-EM further revealed B8 as a class II antibody binding trimeric RBDs in 3-up or 2-up/1-down conformation. Neutralizing dIgA, therefore, may engage an unexpected mode of SARS-CoV-2 nasal infection and injury.
External linksEmerg Microbes Infect / PubMed:37542391 / PubMed Central
MethodsEM (single particle)
Resolution2.65 - 3.11 Å
Structure data

32497

7wh8

EMDB-32497, PDB-7wh8:
SARS-CoV-2 spike in complex with the ZB8 neutralizing antibody Fab (focused refinement on Fab-RBD)
Method: EM (single particle) / Resolution: 3.11 Å

32498

7whb

EMDB-32498, PDB-7whb:
SARS-CoV-2 spike in complex with the ZB8 neutralizing antibody Fab (3U)
Method: EM (single particle) / Resolution: 2.67 Å

32499

7whd

EMDB-32499, PDB-7whd:
SARS-CoV-2 spike in complex with the ZB8 neutralizing antibody Fab (2u1d)
Method: EM (single particle) / Resolution: 2.65 Å

Chemicals

ChemComp-NAG:
2-acetamido-2-deoxy-beta-D-glucopyranose

Source
  • homo sapiens (human)
  • severe acute respiratory syndrome coronavirus 2
KeywordsIMMUNE SYSTEM/VIRAL PROTEIN / SARS-CoV-2 spike / receptor binding domain / antibody / VIRAL PROTEIN / IMMUNE SYSTEM-VIRAL PROTEIN complex / VIRAL PROTEIN/IMMUNE SYSTEM / VIRAL PROTEIN-IMMUNE SYSTEM complex

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