Abstract:
:We have described three mutant strains of Pseudorabies virus that contain mutations in the signal sequence coding region of a nonessential envelope glycoprotein, gIII. The alterations disrupt, truncate, or eliminate the hydrophobic core domain of the signal sequence. Each mutant was assayed for its ability to promote the translocation of gIII across the endoplasmic reticulum membrane and the subsequent localization of the mature form of the glycoprotein to the infected cell surface or the virus envelope. Our results confirm and extend findings in other systems that the overall hydrophobicity of the signal sequence core region is a major determinant of translocation efficiency. We were unable to correlate simply the length of the core or the average hydrophobicity of core residues with export efficiency. Because our work involved the use of infectious virus mutants, we were able to identify a virus defect associated with a complete block in gIII export. This defect will facilitate a pseudo-reversion analysis of gIII signal sequence function.
journal_name
Virus Genesjournal_title
Virus genesauthors
Ryan P,Robbins A,Whealy M,Enquist LWdoi
10.1007/BF01702345subject
Has Abstractpub_date
1993-02-01 00:00:00pages
5-21issue
1eissn
0920-8569issn
1572-994Xjournal_volume
7pub_type
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