TY - JOUR
T1 - 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)
AU - Person, Stanley
AU - Desai, Prashant
N1 - Funding Information:
This research project was supported by Public Health Service Grant AI33077. This is the first publication of research findings since our move to the Johns Hopkins Medical School. We are grateful for all the efforts that Professor Wade Gibson and his laboratory colleagues have made and continue to make on our behalf, including the sharing of ideas and facilities. We hope that our collaboration with him will become as productive for him as it already is for us.
PY - 1998/3/1
Y1 - 1998/3/1
N2 - Previously we reported that null mutant viruses of UL19 (VP5) or of UL18 (VP23), essential components of herpes simplex virus type 1 (HSV-1) capsid shells, do not form precursor capsid structures as judged by sedimentation and electron microscope analysis. A goal of the present experiments was to isolate a null mutant virus for the remaining essential component of capsid shells, VP19C, encoded by the UL38 open reading frame (ORF). Furthermore, we wished to determine if a virus altered in the UL26 maturation cleavage site at residues 610 and 611 produced a lethal phenotype. Therefore, we decided to isolate cell lines that encode and express multiple capsid genes. Several cell lines were isolated by transformation of Veto cells and one designated C32 expressed all of the essential capsid proteins. Using this cell line we isolated a null mutant virus in the UL38 ORF and a mutant virus that was altered at residues 610 and 611 of the UL26 and UL26.5 gene products. We found that the null mutant in VP19C did not form a detectable product as judged by sedimentation and electron microscope analyses following infection of nonpermissive cells. The mutant virus altered at the UL26 maturation site resulted in the accumulation of B capsids. Therefore, cleavage at this site was essential for the maturation of B capsids into C capsids. interestingly, the absence of cleavage at the maturation site was required for the retention of VP24 in the capsid.
AB - Previously we reported that null mutant viruses of UL19 (VP5) or of UL18 (VP23), essential components of herpes simplex virus type 1 (HSV-1) capsid shells, do not form precursor capsid structures as judged by sedimentation and electron microscope analysis. A goal of the present experiments was to isolate a null mutant virus for the remaining essential component of capsid shells, VP19C, encoded by the UL38 open reading frame (ORF). Furthermore, we wished to determine if a virus altered in the UL26 maturation cleavage site at residues 610 and 611 produced a lethal phenotype. Therefore, we decided to isolate cell lines that encode and express multiple capsid genes. Several cell lines were isolated by transformation of Veto cells and one designated C32 expressed all of the essential capsid proteins. Using this cell line we isolated a null mutant virus in the UL38 ORF and a mutant virus that was altered at residues 610 and 611 of the UL26 and UL26.5 gene products. We found that the null mutant in VP19C did not form a detectable product as judged by sedimentation and electron microscope analyses following infection of nonpermissive cells. The mutant virus altered at the UL26 maturation site resulted in the accumulation of B capsids. Therefore, cleavage at this site was essential for the maturation of B capsids into C capsids. interestingly, the absence of cleavage at the maturation site was required for the retention of VP24 in the capsid.
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U2 - 10.1006/viro.1997.9005
DO - 10.1006/viro.1997.9005
M3 - Article
C2 - 9501049
AN - SCOPUS:0032029782
SN - 0042-6822
VL - 242
SP - 193
EP - 203
JO - Virology
JF - Virology
IS - 1
ER -