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 language | English (US) |
|---|---|
| Pages (from-to) | 6833-6838 |
| Number of pages | 6 |
| Journal | Journal of Virology |
| Volume | 69 |
| Issue number | 11 |
| State | Published - 1995 |
| Externally published | Yes |
Fingerprint
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 journal › Article
}
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 -