scholarly journals Membrane Permeability Induced by Hepatitis A Virus Proteins 2B and 2BC and Proteolytic Processing of HAV 2BC

Virology ◽  
1998 ◽  
Vol 252 (1) ◽  
pp. 218-227 ◽  
Author(s):  
Monika Jecht ◽  
Christian Probst ◽  
Verena Gauss-Müller
Keyword(s):  
Membrane Permeability ◽  
Hepatitis A ◽  
Hepatitis A Virus ◽  
Proteolytic Processing ◽  
Virus Proteins

scholarly journals Solubility as a limiting factor for expression of hepatitis A virus proteins in insect cell-baculovirus system

2016 ◽  
Vol 111 (8) ◽  
pp. 535-538
Author(s):  
Haroldo Cid da Silva Junior ◽  
Cristiane Pinheiro Pestana ◽  
Ricardo Galler ◽  
Marco Alberto Medeiros
Keyword(s):  
Insect Cell ◽  
Hepatitis A ◽  
Hepatitis A Virus ◽  
Limiting Factor ◽  
Baculovirus System ◽  
Virus Proteins

scholarly journals Cell-free translation and proteolytic processing of the hepatitis A virus polyprotein

1993 ◽  
Vol 74 (4) ◽  
pp. 677-683 ◽  
Author(s):  
D. Jurgensen ◽  
Y. Y. Kusov ◽  
M. Facke ◽  
H.-G. Krausslich ◽  
V. Gauss-Muller
Keyword(s):  
Hepatitis A ◽  
Hepatitis A Virus ◽  
Proteolytic Processing ◽  
Free Translation ◽  
Virus Polyprotein

Prediction of Secondary Structure, Spatial Organization and Distribution of Antigenic Determinants for Hepatitis A Virus Proteins

1987 ◽  
Vol 5 (2) ◽  
pp. 447-458 ◽  
Author(s):  
Vadim V. Mesyanzhinov ◽  
Elena N. Peletskaya ◽  
Viktor M. Zhdanov ◽  
Alexander V. Efimov ◽  
Alexey V. Finkelstein ◽  
...  
Keyword(s):  
Secondary Structure ◽  
Hepatitis A ◽  
Spatial Organization ◽  
Hepatitis A Virus ◽  
Antigenic Determinants ◽  
Prediction Of Secondary Structure ◽  
Virus Proteins

scholarly journals Improving Proteolytic Cleavage at the 3A/3B Site of the Hepatitis A Virus Polyprotein Impairs Processing and Particle Formation, and the Impairment Can Be Complemented intrans by 3AB and 3ABC

1999 ◽  
Vol 73 (12) ◽  
pp. 9867-9878 ◽  
Author(s):  
Yuri Kusov ◽  
Verena Gauss-Müller
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Cleavage Site ◽  
Hepatitis A ◽  
Hepatitis A Virus ◽  
Particle Formation ◽  
Proteolytic Processing ◽  
Cleavage Sites ◽  
Structural Protein ◽  
Hydrophobic Domain

ABSTRACT The orchestrated liberation of viral proteins by 3Cpro-mediated proteolysis is pivotal for gene expression by picornaviruses. Proteolytic processing is regulated either by the amino acid sequence at the cleavage site of the substrate or by cofactors covalently or noncovalently linked to the viral proteinase. To determine the role of the amino acid sequence at cleavage sites 3A/3B and 3B/3C that are essential for the liberation of 3Cpro from its precursors and to assess the function of the stable processing intermediates 3AB and 3ABC, we studied the effect of cleavage site mutations on hepatitis A virus (HAV) polyprotein processing, particle formation, and replication. Using the recombinant vaccinia virus system, we showed that the normally retarded cleavage at the 3A/3B junction can be improved by altering the amino acid sequence at the scissile bond such that it matches the preferred HAV 3C cleavage sites. In contrast to the processing products of the wild-type polyprotein, 3ABC was no longer detectable in the mutant. VP0 and VP3 were generated less efficiently, implying that processing of the structural protein precursor P1-2A depends on the presence of stable 3ABC and/or 3AB. In addition, cleavage of 2BC was impaired in 3AB/3ABC-deficient mutants. Formation of HAV particles was not affected in mutants with blocked 3A/3B and/or 3B/3C cleavage sites. However, 3ABC-deficient mutants produced small numbers of HAV particles, which could be augmented by coexpressing 3AB or 3ABC. The hydrophobic domain of 3A that has been proposed to mediate membrane anchorage of the replication complex was crucial for restoration of defective particle formation. In vitro transcripts of the various cleavage site mutants were unable to initiate an infectious cycle, and no progeny viruses were obtained even after blind passages. Taken together, the data suggest that accumulation of uncleaved HAV 3AB and/or 3ABC is pivotal for both viral replication and efficient particle formation.

Hepatitis A Virus Proteins

Intervirology ◽  
1999 ◽  
Vol 42 (2-3) ◽  
pp. 63-68 ◽  
Author(s):  
Atsuko Totsuka ◽  
Yasuo Moritsugu
Keyword(s):  
Hepatitis A ◽  
Hepatitis A Virus ◽  
Virus Proteins

Mutational modifications of hepatitis A virus proteins 2B and 2C described for cell culture-adapted and attenuated virus are present in wild-type virus populations

2014 ◽  
Vol 159 (10) ◽  
pp. 2699-2704 ◽  
Author(s):  
Rebecca Weilandt ◽  
Dajana Paulmann ◽  
Kore Schlottau ◽  
Angelika Vallbracht ◽  
Andreas Dotzauer
Keyword(s):  
Cell Culture ◽  
Hepatitis A ◽  
Hepatitis A Virus ◽  
Wild Type Virus ◽  
Type Virus ◽  
Wild Type ◽  
Attenuated Virus ◽  
Virus Proteins

scholarly journals Processing of Proteinase Precursors and Their Effect on Hepatitis A Virus Particle Formation

1998 ◽  
Vol 72 (10) ◽  
pp. 8013-8020 ◽  
Author(s):  
Christian Probst ◽  
Monika Jecht ◽  
Verena Gauss-Müller
Keyword(s):  
Hepatitis A ◽  
Hepatitis A Virus ◽  
Particle Formation ◽  
Proteolytic Processing ◽  
Structural Proteins ◽  
Genome Replication ◽  
Polyprotein Processing ◽  
Capsid Formation ◽  
Viral Particles ◽  
Differential Action

ABSTRACT Proteolytic processing of the picornaviral polyprotein mediated by the differential action of virus-encoded proteinase(s) is pivotal to both RNA genome replication and capsid formation. Possibly to enlarge the array of viral proteins, picornaviral polyprotein processing results in intermediate and mature products which apparently have distinct functions within the viral life cycle. For hepatitis A virus (HAV), we report here on the autoproteolysis of precursor polypeptides comprising the only viral proteinase, 3Cpro, and on their role in viral particle formation. Following transient expression of a nested set of 3Cpro-containing proteins (P3, 3ABC, 3BCD, 3CD, 3BC, and 3C) in eukaryotic cells, the extent of processing was determined by analyzing the cleavage products. The 3C/3D site was more efficiently cleaved than those at the 3A/3B and 3B/3C sites, leading to the accumulation of the intermediate product 3ABC. In the absence of 3A from the precursor, cleavage at the 3B/3C site was further reduced and a switch to an alternative 3C/3D site was observed. Coexpression of various parts of P3 with the precursor of the viral structural proteins P1-2A showed that all 3C-containing intermediates cleaved P1-2A with almost equal efficiency; however, viral particles carrying the neutralizing epitope form much more readily in the presence of the complete P3 domain than with parts of it. These data support the notion that efficient liberation of structural proteins from P1-2A is necessary but not sufficient for productive HAV capsid formation and suggest that the polypeptides flanking 3Cpropromote the assembly of viral particles.

Perinuclear accumulation of hepatitis A virus proteins, RNA, and particles and ultrastructural alterations in infected cells

2001 ◽  
Vol 146 (12) ◽  
pp. 2291-2307 ◽  
Author(s):  
M. H. F. Klinger ◽  
R. Kämmerer ◽  
B. Hornei ◽  
V. Gauss-Müller
Keyword(s):  
Hepatitis A ◽  
Hepatitis A Virus ◽  
Ultrastructural Alterations ◽  
Infected Cells ◽  
Virus Proteins

Detection of hepatitis A virus proteins in infected BS-C-1 cells

Virology ◽  
1991 ◽  
Vol 185 (1) ◽  
pp. 411-418 ◽  
Author(s):  
Wanda S. Updike ◽  
Michael Tesar ◽  
Ellie Ehrenfeld
Keyword(s):  
Hepatitis A ◽  
Hepatitis A Virus ◽  
Virus Proteins
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