Related Experiment Videos
Structural proteins of two different plaque-size phenotypes of fowlpox virus
K Nazerian1, S Dhawale, W S Payne
1U.S. Department of Agriculture, Agricultural Research Service, East Lansing, Michigan 48823.
Abstract:
Structural polypeptides of two plaque-purified variant isolates of fowlpox virus differing in plaque morphology and size were examined by Coomassie blue-staining and immunoblot analysis of purified virions. A total of 30 structural polypeptides were observed, ranging in molecular weight from 14,100 to 122,600. A late polypeptide of 36,400 molecular weight was quite prominent in the small-plaque clone but absent in the large-plaque clone. Two other polypeptides, of 33,700 and 34,800 molecular weight, were present in virions from large-plaque virus and cell lysates of both clones but were absent in the small-plaque virions. These differences were observed whether the viruses were grown in chorioallantoic membrane or in chicken embryo fibroblast cultures. No difference was observed between the growth curves of the two virus clones. Differences observed in the polypeptides of the two viruses may be due to changes in the less conserved regions of viral DNA and may be used for differentiation of virus isolates.
Insights
Structural differences in fowlpox virus (FPV) variants were identified through polypeptide analysis. These variations in FPV structural proteins could aid in distinguishing between different virus isolates.
Area of Science:
- Virology
- Molecular Biology
- Biochemistry
Background:
- Fowlpox virus (FPV) exists in various isolates with differing plaque morphologies.
- Understanding the molecular basis of these variations is crucial for viral differentiation.
Purpose of the Study:
- To analyze and compare the structural polypeptides of two FPV variants with distinct plaque characteristics.
- To identify specific protein differences that could serve as markers for distinguishing FPV isolates.
Main Methods:
- Purified virions from small-plaque and large-plaque FPV variants were analyzed.
- Coomassie blue staining and immunoblot analysis were employed to examine structural polypeptides.
- Molecular weights of polypeptides were determined.
Main Results:
- A total of 30 structural polypeptides were identified, ranging from 14,100 to 122,600 molecular weight.
- A 36,400 MW polypeptide was present in the small-plaque clone but absent in the large-plaque clone.
- Two other polypeptides (33,700 and 34,800 MW) were found in large-plaque virions but not in small-plaque virions.
Conclusions:
- Distinct differences in structural polypeptides exist between FPV variants with different plaque morphologies.
- These protein variations may arise from alterations in less conserved regions of the viral DNA.
- The identified polypeptide differences offer a potential method for differentiating FPV isolates.