Insertions within the hepatitis B virus capsid protein influence capsid formation and RNA encapsidation

B. Beames, R. E. Lanford

Research output: Contribution to journalArticle

20 Citations (Scopus)

Abstract

Hepatitis B virus (HBV) capsid proteins, termed core proteins, with two- to four-amino-acid insertions were assessed for capsid formation, RNA encapsidation, and the ability to support reverse transcription of the pregenome by the polymerase molecule. Velocity sedimentation analysis of insect cell-expressed recombinant core proteins revealed that only two of the nine insertion mutant proteins formed capsids with the tight banding patterns of wild-type capsids. The remaining mutant core proteins were spread over the gradients, suggesting aggregate formation, or at the top of the gradients, suggesting lack of stable capsid formation. The mutant capsid proteins were coexpressed in Huh7 cells with an HBV genome lacking a functional core gene to test for trans complementation of HBV replication. Three of the mutant core proteins formed capsids containing HBV RNA, but only two of these contained reverse-transcribed HBV DNA. While the core protein has shown resiliency in capsid formation following insertion of foreign residues into the major B-cell epitope, several of the small insertions severely reduced the efficiency of capsid formation and inhibited capsid function.

Original languageEnglish (US)
Pages (from-to)6833-6838
Number of pages6
JournalJournal of Virology
Volume69
Issue number11
StatePublished - 1995
Externally publishedYes

Fingerprint

capsid
Hepatitis B virus
Capsid
Capsid Proteins
coat proteins
RNA
Mutant Proteins
Genetic Complementation Test
mutants
proteins
B-Lymphocyte Epitopes
reverse transcription
protein aggregates
Virus Replication
virus replication
Recombinant Proteins
epitopes
Reverse Transcription
B-lymphocytes
Insects

ASJC Scopus subject areas

  • Immunology

Cite this

Insertions within the hepatitis B virus capsid protein influence capsid formation and RNA encapsidation. / Beames, B.; Lanford, R. E.

In: Journal of Virology, Vol. 69, No. 11, 1995, p. 6833-6838.

Research output: Contribution to journalArticle

@article{5917ab7af79e4d588176f5c5d4ffa191,
title = "Insertions within the hepatitis B virus capsid protein influence capsid formation and RNA encapsidation",
abstract = "Hepatitis B virus (HBV) capsid proteins, termed core proteins, with two- to four-amino-acid insertions were assessed for capsid formation, RNA encapsidation, and the ability to support reverse transcription of the pregenome by the polymerase molecule. Velocity sedimentation analysis of insect cell-expressed recombinant core proteins revealed that only two of the nine insertion mutant proteins formed capsids with the tight banding patterns of wild-type capsids. The remaining mutant core proteins were spread over the gradients, suggesting aggregate formation, or at the top of the gradients, suggesting lack of stable capsid formation. The mutant capsid proteins were coexpressed in Huh7 cells with an HBV genome lacking a functional core gene to test for trans complementation of HBV replication. Three of the mutant core proteins formed capsids containing HBV RNA, but only two of these contained reverse-transcribed HBV DNA. While the core protein has shown resiliency in capsid formation following insertion of foreign residues into the major B-cell epitope, several of the small insertions severely reduced the efficiency of capsid formation and inhibited capsid function.",
author = "B. Beames and Lanford, {R. E.}",
year = "1995",
language = "English (US)",
volume = "69",
pages = "6833--6838",
journal = "Journal of Virology",
issn = "0022-538X",
publisher = "American Society for Microbiology",
number = "11",

}

TY - JOUR

T1 - Insertions within the hepatitis B virus capsid protein influence capsid formation and RNA encapsidation

AU - Beames, B.

AU - Lanford, R. E.

PY - 1995

Y1 - 1995

N2 - Hepatitis B virus (HBV) capsid proteins, termed core proteins, with two- to four-amino-acid insertions were assessed for capsid formation, RNA encapsidation, and the ability to support reverse transcription of the pregenome by the polymerase molecule. Velocity sedimentation analysis of insect cell-expressed recombinant core proteins revealed that only two of the nine insertion mutant proteins formed capsids with the tight banding patterns of wild-type capsids. The remaining mutant core proteins were spread over the gradients, suggesting aggregate formation, or at the top of the gradients, suggesting lack of stable capsid formation. The mutant capsid proteins were coexpressed in Huh7 cells with an HBV genome lacking a functional core gene to test for trans complementation of HBV replication. Three of the mutant core proteins formed capsids containing HBV RNA, but only two of these contained reverse-transcribed HBV DNA. While the core protein has shown resiliency in capsid formation following insertion of foreign residues into the major B-cell epitope, several of the small insertions severely reduced the efficiency of capsid formation and inhibited capsid function.

AB - Hepatitis B virus (HBV) capsid proteins, termed core proteins, with two- to four-amino-acid insertions were assessed for capsid formation, RNA encapsidation, and the ability to support reverse transcription of the pregenome by the polymerase molecule. Velocity sedimentation analysis of insect cell-expressed recombinant core proteins revealed that only two of the nine insertion mutant proteins formed capsids with the tight banding patterns of wild-type capsids. The remaining mutant core proteins were spread over the gradients, suggesting aggregate formation, or at the top of the gradients, suggesting lack of stable capsid formation. The mutant capsid proteins were coexpressed in Huh7 cells with an HBV genome lacking a functional core gene to test for trans complementation of HBV replication. Three of the mutant core proteins formed capsids containing HBV RNA, but only two of these contained reverse-transcribed HBV DNA. While the core protein has shown resiliency in capsid formation following insertion of foreign residues into the major B-cell epitope, several of the small insertions severely reduced the efficiency of capsid formation and inhibited capsid function.

UR - http://www.scopus.com/inward/record.url?scp=0028832606&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0028832606&partnerID=8YFLogxK

M3 - Article

C2 - 7474096

AN - SCOPUS:0028832606

VL - 69

SP - 6833

EP - 6838

JO - Journal of Virology

JF - Journal of Virology

SN - 0022-538X

IS - 11

ER -