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Physical mapping of herpes simplex virus-induced polypeptides.
Journal of Virology
|November 1, 1978
Summary
Herpes simplex virus genome mapping reveals that immediate-early, late, phosphorylated, and glycosylated proteins are not restricted to specific DNA regions. This finding impacts our understanding of viral gene function.
Area of Science:
- Virology
- Molecular Biology
- Genetics
Background:
- Herpes simplex virus (HSV) genome organization is complex, with distinct long (L) and short (S) regions.
- Understanding the precise mapping of viral polypeptides is crucial for deciphering viral gene function and replication strategies.
Purpose of the Study:
- To map the positions of various herpes simplex virus type 1/type 2 intertypic recombinant-induced polypeptides within the viral genome.
- To correlate polypeptide map positions with crossover points in recombinant DNAs.
- To determine if specific functional groups of proteins are confined to either the L or S regions of the HSV genome.
Main Methods:
- Analysis of polypeptides induced by 29 HSV type 1/type 2 intertypic recombinants.
- Correlation of polypeptide data with crossover points in recombinant DNAs.
- Labeling of polypeptides using [35S]methionine, [32P]orthophosphate, and [14C]glucosamine.
- Integration of data with previously mapped immediate-early polypeptides.
Main Results:
- Map positions were deduced for 25 methionine-labeled, 11 phosphate-labeled, and 4 glucosamine-labeled polypeptides.
- Immediate-early, late, phosphorylated, and glycosylated proteins were found to map in both the L and S regions of the genome.
- This mapping extends previous findings for immediate-early polypeptides.
Conclusions:
- The functional organization of the herpes simplex virus genome does not restrict immediate-early, late, phosphorylated, or glycosylated proteins to either the L or S regions.
- Viral genes encoding these protein classes are distributed across both major genome segments.
- This suggests a more complex functional compartmentalization than previously assumed for these protein groups.