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Article

Modification of the trypsin cleavage site of rotavirus VP4 to a furin-sensitive form does not enhance replication efficiency.

The Journal of general virology - 1 Dec 2011

Komoto Satoshi, Wakuda Mitsutaka, Ide Tomihiko, Niimi Gen, Maeno Yoshimasa, Higo-Moriguchi Kyoko, Taniguchi Koki

Abstract excerpt

The infectivity of rotavirus (RV) is dependent on an activation process triggered by the proteolytic cleavage of its spike protein VP4. This activation cleavage is performed by exogenous trypsin in the lumen of the intestines in vivo. Here, we report the generation and characterization of a recombinant RV expressing cDNA-derived VP4 with a modified cleavage site (arginine at position 247) recognized by endogenous...

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Source

Identifiers

PMID: 21813706
DOI: 10.1099/vir.0.033886-0

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 5 Sept 2026. Manifest publication-graph-cohort-2026-09-05.1.

Source receipt: pubmed, retrieved 5 Sept 2026.

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