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The UL 15 gene of herpes simplex virus type 1 (HSV-1), like UL 6, UL 17, UL 28, UL 32, and UL 33, is required for cleavage of concatameric DNA into genomic lengths and for packaging of cleaved genomes into preformed capsids. A previous study indicated that the UL 15 gene encodes minor capsid proteins. In the present study, we have shown that the amino-terminal 509 amino acids of the UL 15-encoded protein are sufficient to confer capsid association inasmuch as a carboxyl-terminally truncated form of the UL 15-encoded protein with anM r of approximately 55,000 readily associated with capsids. This and previous studies have shown that, whereas three UL 15-encoded proteins with apparentM r s of 83,000, 80,000, and 79,000 associated with wild-type B capsids, only the full-length 83,000-M r protein associated with B capsids purified from cells infected with viruses lacking functional UL 6, UL 17, UL 28, UL 32, and UL 33 genes (B. Salmon and J. D. Baines, J. Virol. 72:3045–3050, 1998). Thus, all viral mutants that fail to cleave viral DNA into genomic-length molecules also fail to produce capsid-associated UL 15 80,000- and 79,000-M r proteins. In contrast, the 80,000- and 79,000-M r proteins were readily detected in capsids purified from cells infected with a UL 25 null virus that cleaves, but does not package, DNA. The conclusion that the amino terminus of the 83,000-M r protein is truncated to produce the 80,000- and/or 79,000-M r protein was supported by the following observations. (i) Whereas the C termini of the 83,000-, 80,000-, and 79,000-M r proteins are identical, immunoreactivity dependent on the first 35 amino acids of the UL 15 83,000-M r protein was absent from the 80,000- and 79,000-M r proteins. (ii) The 79,000- and 80,000-M r proteins were detected in capsids from cells infected with HSV-1(UL 15M36V), an engineered virus encoding valine rather than methionine at codon 36. Thus, initiation at codon 36 is unlikely to account for production of the 80,000- and/or 79,000-M r protein. Taken together, these data strongly suggest that capsid-associated UL 15-encoded protein is proteolytically cleaved near the N terminus and indicate that this modification is tightly linked to maturation of genomic DNA.

journal of virology

Proteolytic Cleavage of the Amino Terminus of the U <sub>L</sub> 15 Gene Product of Herpes Simplex Virus Type 1 Is Coupled with Maturation of Viral DNA into Unit-Length Genomes

Proteolytic Cleavage of the Amino Terminus of the U L 15 Gene Product of Herpes Simplex Virus Type 1 Is Coupled with Maturation of Viral DNA into Unit-Length Genomes

Proteolytic Cleavage of the Amino Terminus of the U _L 15 Gene Product of Herpes Simplex Virus Type 1 Is Coupled with Maturation of Viral DNA into Unit-Length Genomes