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Binding of a bovine ultralong CDRH3 to the SARS-CoV RBD

ABSTRACT: Here, we have used a SARS-naïve, bovine ultralong CDRH3 library to isolate a bovine paratope that engages the SARS-CoV and SARS-CoV-2 receptor-binding domain (RBD). This scFv (B9-scFv) neutralises viruses pseudo-typed with SARS-CoV Spike protein. Using differential hydrogen-deuterium exchange mass spectrometry and site-directed mutagenesis, we demonstrate that this CDRH3 recognises a conserved, cryptic epitope.

INSTRUMENT(S): Synapt MS

ORGANISM(S): Bos Taurus (bovine)

SUBMITTER: Antonio Calabrese

LAB HEAD: Antonio Calabrese

PROVIDER: PXD032965 | Pride | 2023-03-11

REPOSITORIES: Pride

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			Action	DRS
	HDX_sars_b9.DnX	Other
	fbstcm_220128_hdx1_01.raw.zip	Raw
	fbstcm_220128_hdx1_03.raw.zip	Raw
	fbstcm_220128_hdx1_05.raw.zip	Raw
	fbstcm_220128_hdx1_07.raw.zip	Raw

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Publications

A bovine antibody possessing an ultralong complementarity-determining region CDRH3 targets a highly conserved epitope in sarbecovirus spike proteins.

Burke Matthew J MJ Scott James N F JNF Minshull Thomas C TC Gao Zeqian Z Manfield Iain I Savic Sinisa S Stockley Peter G PG Calabrese Antonio N AN Boyes Joan J

The Journal of biological chemistry 20221020 12

Broadly neutralizing antibodies have huge potential as novel antiviral therapeutics due to their ability to recognize highly conserved epitopes that are seldom mutated in viral variants. A subset of bovine antibodies possess an ultralong complementarity-determining region (CDR)H3 that is highly adept at recognizing such conserved epitopes, but their reactivity against Sarbecovirus Spike proteins has not been explored previously. Here, we use a SARS-naïve library to isolate a broadly reactive bov ...[more]

PMID: 36272646

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