Literature DB >> 2823462

Genetic and phenotypic characterization of mutants in four essential genes that map to the left half of HSV-1 UL DNA.

S K Weller1, E P Carmichael, D P Aschman, D J Goldstein, P A Schaffer.   

Abstract

Several HSV-1 proteins including the major capsid protein (VP5), two minor capsid proteins (VP11-12 and VP18.8), the alkaline nuclease and glycoprotein gH have been reported to be encoded by the left-most one-third of HSV-1 UL DNA. In this paper, we present physical mapping data and phenotypic analysis of six ts mutants whose mutations lie within this region and which collectively represent four functional complementation groups (1-6, 1-7, 1-10, and 1-26). In this study, mutants in complementation group 1-10 were found to be defective in the synthesis of viral DNA, late viral polypeptides, and the formation of mature capsid-like structures--properties characteristic of other ts mutants defective in functions required for viral DNA synthesis. Two DNA-positive mutants in complementation group 1-7 fail to induce capsid formation and probably possess mutations in coding sequences for VP5. Mutants in two other complementation groups (1-6 and 1-26) synthesize significant levels of viral DNA, late polypeptides, and capsids. The functions of the gene products represented by these mutants remain to be determined.

Entities:  

Mesh:

Substances:

Year:  1987        PMID: 2823462     DOI: 10.1016/0042-6822(87)90186-3

Source DB:  PubMed          Journal:  Virology        ISSN: 0042-6822            Impact factor:   3.616


  41 in total

1.  DNA cleavage and packaging proteins encoded by genes U(L)28, U(L)15, and U(L)33 of herpes simplex virus type 1 form a complex in infected cells.

Authors:  Philippa M Beard; Naomi S Taus; Joel D Baines
Journal:  J Virol       Date:  2002-05       Impact factor: 5.103

2.  The conserved helicase motifs of the herpes simplex virus type 1 origin-binding protein UL9 are important for function.

Authors:  R Martinez; L Shao; S K Weller
Journal:  J Virol       Date:  1992-11       Impact factor: 5.103

3.  The UL8 subunit of the herpes simplex virus helicase-primase complex is required for efficient primer utilization.

Authors:  G Sherman; J Gottlieb; M D Challberg
Journal:  J Virol       Date:  1992-08       Impact factor: 5.103

4.  Involvement of the portal at an early step in herpes simplex virus capsid assembly.

Authors:  William W Newcomb; Fred L Homa; Jay C Brown
Journal:  J Virol       Date:  2005-08       Impact factor: 5.103

5.  Dynamic interactions of the UL16 tegument protein with the capsid of herpes simplex virus.

Authors:  David G Meckes; John W Wills
Journal:  J Virol       Date:  2007-09-12       Impact factor: 5.103

6.  The UL5 gene of herpes simplex virus type 1: isolation of a lacZ insertion mutant and association of the UL5 gene product with other members of the helicase-primase complex.

Authors:  L A Zhu; S K Weller
Journal:  J Virol       Date:  1992-01       Impact factor: 5.103

7.  Interaction domains of the UL16 and UL21 tegument proteins of herpes simplex virus.

Authors:  Amy L Harper; David G Meckes; Jacob A Marsh; Michael D Ward; Pei-Chun Yeh; Nicholas L Baird; Carol B Wilson; O John Semmes; John W Wills
Journal:  J Virol       Date:  2009-12-30       Impact factor: 5.103

8.  Herpes simplex virus type 1 alkaline nuclease is required for efficient processing of viral DNA replication intermediates.

Authors:  R Martinez; R T Sarisky; P C Weber; S K Weller
Journal:  J Virol       Date:  1996-04       Impact factor: 5.103

9.  The herpes simplex virus type 1 U(L)17 gene encodes virion tegument proteins that are required for cleavage and packaging of viral DNA.

Authors:  B Salmon; C Cunningham; A J Davison; W J Harris; J D Baines
Journal:  J Virol       Date:  1998-05       Impact factor: 5.103

10.  Helicase-primase complex of herpes simplex virus type 1: a mutation in the UL52 subunit abolishes primase activity.

Authors:  D K Klinedinst; M D Challberg
Journal:  J Virol       Date:  1994-06       Impact factor: 5.103

View more

北京卡尤迪生物科技股份有限公司 © 2022-2023.