scholarly journals Effect of Mutations in the Small Envelope Protein of Hepatitis B Virus on Assembly and Secretion of Hepatitis Delta Virus

Virology ◽  
1998 ◽  
Vol 251 (1) ◽  
pp. 176-186 ◽  
Author(s):  
Sarah Jenna ◽  
Camille Sureau
2007 ◽  
Vol 81 (8) ◽  
pp. 4343-4347 ◽  
Author(s):  
Severin Gudima ◽  
Anja Meier ◽  
Roland Dunbrack ◽  
John Taylor ◽  
Volker Bruss

ABSTRACT Previous studies have attempted to clarify the roles of the pre-S1 and pre-S2 domains of the large envelope protein of hepatitis B virus (HBV) in attachment and entry into susceptible cells. Difficulties arise in that these domains contain regions involved in the nucleocapsid assembly of HBV and overlapping with the coding regions of the viral polymerase and RNA sequences required for reverse transcription. Such difficulties can be circumvented with hepatitis delta virus (HDV), which needs the HBV large envelope protein only for infectivity. Thus, mutated HBV envelope proteins were examined for their effects on HDV infectivity. Changing the C-terminal region of pre-S1 critical for HBV assembly allowed the envelopment of HDV and had no effect on infectivity in primary human hepatocytes. Similarly, a deletion of the 12 amino acids of a putative translocation motif (TLM) in pre-S2 had no effect. Thus, these two regions are not necessary for HDV infectivity and, by inference, are not needed for HBV attachment and entry into susceptible cells.


1999 ◽  
Vol 73 (4) ◽  
pp. 3351-3358 ◽  
Author(s):  
Sarah Jenna ◽  
Camille Sureau

ABSTRACT The carboxyl-terminal domain of the small (S) envelope protein of hepatitis B virus was subjected to mutagenesis to identify sequences important for the envelopment of the nucleocapsid during morphogenesis of hepatitis delta virus (HDV) virions. The mutations consisted of carboxyl-terminal truncations of 4 to 64 amino acid residues and small combined deletions and insertions spanning the entire hydrophobic domain between residues 163 and 224. Truncation of as few as 14 residues partially inhibited glycosylation and secretion of S and prevented assembly or stability of HDV virions. Short internal combined deletions and insertions were tolerated for secretion of subviral particles with the exceptions of those affecting residues 164 to 173 and 219 to 223. However, mutants competent for subviral particle secretion had a reduced capacity for HDV assembly compared to that of the wild type. One exception was a mutant carrying a deletion of residues 214 to 218, which exhibited a twofold increase in HDV assembly (or stability), whereas deletions of residues 179 to 183, 194 to 198, and 199 to 203 were the most inhibitory. Substitutions of single amino acids between residues 194 and 198 demonstrated that HDV assembly deficiency could be assigned to the replacement of the tryptophan residue at position 196. We concluded that assembly of stable HDV particles requires a specific function of the carboxyl terminus of S which is mediated at least in part by Trp-196.


2021 ◽  
Author(s):  
Kasthuri Prakash ◽  
Simon B. Larsson ◽  
Gustaf E. Rydell ◽  
Johan Ringlander ◽  
Catarina Skoglund ◽  
...  

Digestion ◽  
1993 ◽  
Vol 54 (1) ◽  
pp. 9-14
Author(s):  
Nicola Napoli ◽  
Giorgio Fiore ◽  
Giacomo Fera ◽  
Angela Modugno ◽  
Gianluigi Giannelli ◽  
...  

2020 ◽  
Vol 73 ◽  
pp. S834-S835
Author(s):  
Benoît Lacombe ◽  
Julie Lucifora ◽  
Camille Ménard ◽  
Michelet Maud ◽  
Adrien Foca ◽  
...  

Sign in / Sign up

Export Citation Format

Share Document