Second-site mutations encoding residues 34 and 78 of the major capsid protein (VP5) of herpes simplex virus type 1 are important for overcoming a blocked maturation cleavage site of the capsid scaffold proteins

Virology

Volumn 278, Issue 1, 2000, Pages 217-226

  Warner, Susan C ^a   Desai, Prashant ^a   Person, Stanley ^a  

^a JOHNS HOPKINS UNIVERSITY SCHOOL OF MEDICINE   (United States)

Author keywords

Capsid; Capsid assembly; Herpesvirus; HSV 1; Major capsid protein; Second site mutation; VP5

Indexed keywords

ALANINE; CAPSID PROTEIN; DNA; GENE PRODUCT; SERINE PROTEINASE; VALINE;

ARTICLE; HERPES SIMPLEX VIRUS 1; MUTATION; NONHUMAN; OPEN READING FRAME; POLYACRYLAMIDE GEL ELECTROPHORESIS; PRIORITY JOURNAL; VIRUS CAPSID;

DNA VIRUSES; HERPES; HERPESVIRIDAE; HUMAN HERPESVIRUS 1; MIRIDAE; STAPHYLOCOCCUS PHAGE 187;

EID: 0034610231     PISSN: 00426822     EISSN: None     Source Type: Journal    
DOI: 10.1006/viro.2000.0657     Document Type: Article

References (21)

1. Structural analysis of the capsid polypeptides of herpes simplex virus types 1 and 2
2. Mutations in herpes simplex virus type 1 genes encoding VP5 and VP23 abrogate capsid formation and cleavage of replicated DNA
3. Herpes simplex virus type 1 VP26 is not essential for replication in cell culture but influences production of infectious virus in the nervous system of infected mice
4. Molecular interactions between the HSV-1 capsid proteins as measured by the yeast two-hybrid system
5. Second-site mutations in the N-terminus of the major capsid protein (VPS) overcome a block at the maturation cleavage site of the capsid scaffold proteins of herpes simplex virus type 1
6. Identification of the herpes simplex virus-1 protease cleavage sites by direct sequence analysis of autoproteolytic cleavage products
7. Proteins specified by herpes simplex virus. 8. Characterization and composition of multiple capsid forms of subtypes 1 and 2
8. Isolation of a nucleocapsid polypeptide of herpes simplex virus types 1 and 2 possessing immunologically type-specific and cross-reactive determinants
9. Identification of a minimal hydrophobic domain in the herpes simplex virus type 1 scaffolding protein which is required for interaction with the major capsid protein
10. The 25 amino acid residues at the carboxy terminus of the herpes simplex virus type 1 UL26.5 protein are required for the formation of the capsid shell around the scaffold
11. Characterization of the protease and other products of amino-terminus-proximal cleavage of the herpes simplex virus 1 UL26 protein
12. The herpes simplex virus 1 gene encoding a protease also contains within its coding domain the gene encoding the more abundant substrate
13. The complete DNA sequence of the long unique region in the genome of herpes simplex virus type 1
14. Capsids are formed in a mutant virus blocked at the maturation site of the UL26 and UL26.5 open reading frames of herpes simplex virus type 1 but are not formed in a null mutant of UL38 (VP19C)
15. Processing of the herpes simplex virus assembly protein ICP35 near its carboxy terminal end requires the product of the whole of the UL26 reading frame
16. Separate functional domains of the herpes simplex virus type 1 protease: Evidence for cleavage inside capsids
17. Prediction of protein secondary structure at better than 70% accuracy
18. Assembly of the herpes simplex virus capsid: Requirement for the carboxyl-terminal twenty-five amino acids of the proteins encoded by the UL26 and UL26.5 genes
19. Autoproteolysis of herpes simplex virus type 1 protease releases an active catalytic domain found in intermediate capsid particles
20. A herpesvirus maturational proteinase, assemblin: Identification of its gene, putative active site domain, and cleavage site
21. Seeing the herpesvirus capsid at 8.5 Å