Literature DB >> 6330987

Histone H3 modification in BHK cells infected with foot-and-mouth disease virus.

P R Grigera, S G Tisminetzky.   

Abstract

Infection of BHK cells with foot-and-mouth disease virus (FMDV) causes a thorough change in the electrophoretic profile of whole nuclear histones. It consists in the disappearance of histone H3 and the appearance of a new polypeptide (Pi) which migrates between histones H2A and H4 on SDS-polyacrylamide gels. Protein Pi is detected at 2 hr postinfection (pi), the time in which viral RNA synthesis begins to increase, and reaches equimolecular amounts with the remaining core histones 1 hr later, when the disappearance of histone H3 is almost complete. Labeling of cells prior to infection demonstrates that Pi is not a novo product but the result of a viral-induced processing of a host precursor synthetized beforehand. Protein Pi comigrates with histone H2A/B in acetic acid/urea polyacrylamide gels and it shares common major peptides with histone H3 under controlled proteolysis with protease V8 or trypsin. The mononucleosomal and nucleosomal DNA pattern analysis after micrococcal nuclease treatment of nuclei from infected and mock-infected cells did not show any significant differences even though after 3 hr (p.i.), protein Pi replaces histone H3 in the nucleosomal structure. It was concluded that FMDV infection is responsible for a specific modification in the nucleus of infected cells which leads, after 3 hr (p.i.), to a complete histone H3 protein Pi transition in the nucleosomes.

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Year:  1984        PMID: 6330987     DOI: 10.1016/0042-6822(84)90243-5

Source DB:  PubMed          Journal:  Virology        ISSN: 0042-6822            Impact factor:   3.616


  15 in total

Review 1.  Foot-and-mouth disease.

Authors:  Marvin J Grubman; Barry Baxt
Journal:  Clin Microbiol Rev       Date:  2004-04       Impact factor: 26.132

2.  Degradation of cellular proteins during poliovirus infection: studies by two-dimensional gel electrophoresis.

Authors:  A Urzainqui; L Carrasco
Journal:  J Virol       Date:  1989-11       Impact factor: 5.103

3.  Viral subversion of host functions for picornavirus translation and RNA replication.

Authors:  Amanda J Chase; Bert L Semler
Journal:  Future Virol       Date:  2012-02       Impact factor: 1.831

Review 4.  Proteolytic clipping of histone tails: the emerging role of histone proteases in regulation of various biological processes.

Authors:  Gajendra Kumar Azad; Raghuvir S Tomar
Journal:  Mol Biol Rep       Date:  2014-05       Impact factor: 2.316

5.  Foot-and-mouth disease virus protease 3C induces specific proteolytic cleavage of host cell histone H3.

Authors:  M M Falk; P R Grigera; I E Bergmann; A Zibert; G Multhaup; E Beck
Journal:  J Virol       Date:  1990-02       Impact factor: 5.103

6.  Residues within the Foot-and-Mouth Disease Virus 3Dpol Nuclear Localization Signal Affect Polymerase Fidelity.

Authors:  Anna Kloc; Devendra K Rai; Douglas P Gladue; Elizabeth Schafer; Mary Kenney; Elizabeth Rieder
Journal:  J Virol       Date:  2020-08-17       Impact factor: 5.103

7.  Proteolytic cleavage of host proteins by the Group IV viral proteases of Venezuelan equine encephalitis virus and Zika virus.

Authors:  Elaine M Morazzani; Jaimee R Compton; Dagmar H Leary; Angela V Berry; Xin Hu; Juan J Marugan; Pamela J Glass; Patricia M Legler
Journal:  Antiviral Res       Date:  2019-02-10       Impact factor: 10.103

8.  Serological probes for some foot-and-mouth disease virus nonstructural proteins.

Authors:  M Tesar; H G Berger; O Marquardt
Journal:  Virus Genes       Date:  1989-09       Impact factor: 2.332

Review 9.  Picornaviruses and nuclear functions: targeting a cellular compartment distinct from the replication site of a positive-strand RNA virus.

Authors:  Dylan Flather; Bert L Semler
Journal:  Front Microbiol       Date:  2015-06-18       Impact factor: 5.640

10.  Antiviral efficacy of short-hairpin RNAs and artificial microRNAs targeting foot-and-mouth disease virus.

Authors:  Anabella Currá; Marco Cacciabue; María José Gravisaco; Sebastián Asurmendi; Oscar Taboga; María I Gismondi
Journal:  PeerJ       Date:  2021-06-09       Impact factor: 2.984

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