Characterization of a human astrovirus serotype 2 structural protein (VP26) that contains an epitope involved in virus neutralization.

Abstract:

:An improved purification procedure for human astrovirus serotype 2 (H-Ast2) has facilitated the isolation of a neutralizing monoclonal antibody (PL-2) directed against one of the major structural proteins (VP26) of H-Ast2. A minor component (VP29) of the virus particles is also recognized by PL-2 antibody. Immunofluorescent staining indicated that VP26 (and/or VP29) has mainly a cytoplasmic location in LLCMK2-infected cells. Immunoelectron microscopy demonstrated that the PL-2 epitope was present in the surface of astrovirus particles. Pulse-chase radiolabeling and immunoprecipitation of H-Ast2-infected cell extracts identified a P86 precursor of VP26. Several intermediate protein species (P74 to P35) that shared the PL-2 epitope were also identified in the infected cells. Finally, partial N-terminal sequencing of VP29 and VP26 polypeptides demonstrated that they originated by alternative processing of P86 after residues 361 and 394, respectively. These results corroborate the location of the astrovirus structural genes at the 3' end of the viral genome included in the previously identified 2.8-kb subgenomic RNA.

journal_name

Virology

journal_title

Virology

authors

Sanchez-Fauquier A,Carrascosa AL,Carrascosa JL,Otero A,Glass RI,Lopez JA,San Martin C,Melero JA

doi

10.1006/viro.1994.1296

subject

Has Abstract

pub_date

1994-06-01 00:00:00

pages

312-20

issue

2

eissn

0042-6822

issn

1096-0341

pii

S0042-6822(84)71296-7

journal_volume

201

pub_type

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