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Published on: June 14, 2022
Positively selected sites on the surface glycoprotein (G) of infectious hematopoietic necrosis virus
Scott E LaPatra1, Caryn Evilia2, Vern Winston2
1Clear Springs Foods Inc., PO Box 712, Buhl, ID 83316, USA.
Abstract:
Mutations in the surface glycoprotein (G) of infectious hematopoietic necrosis virus (IHNV), a rhabdovirus that causes significant losses in hatcheries raising salmonid fish, were studied. A 303 nt segment (mid-G region) of this protein from 88 Idaho isolates of IHNV was sequenced. Evidence of positive selection at individual codon sites was estimated by using a Bayesian method (MrBayes). A software algorithm (CPHmodels) was used to construct a three-dimensional (3D) representation of the IHNV protein. The software identified structural homologies between the IHNV G protein and the surface glycoprotein of vesicular stomatitis virus (VSV) and used the VSV structure as a template for predicting the IHNV structure. The amino acids predicted to be under positive selection were mapped onto the proposed IHNV 3D structure and appeared at sites on the surface of the protein where antigen-antibody interaction should be possible. The sites identified as being under positive selection on the IHNV protein corresponded to those reported by others as active sites of mutation for IHNV, and also as antigenic sites on VSV. Knowledge of the sites where genetic variation is positively selected enables a better understanding of the interaction of the virus with its host, and with the host immune system. This information could be used to develop strategies for vaccine development for IHNV, as well as for other viruses.
Insights
Mutations in infectious hematopoietic necrosis virus (IHNV) surface glycoprotein were analyzed. Positively selected sites, identified on the protein
Area of Science:
- Virology
- Molecular Biology
- Immunology
Background:
- Infectious hematopoietic necrosis virus (IHNV) causes significant losses in salmonid fish hatcheries.
- The surface glycoprotein (G) is crucial for IHNV infectivity and host interaction.
- Understanding genetic variation in IHNV is vital for disease management and vaccine development.
Purpose of the Study:
- To investigate mutations in the IHNV surface glycoprotein (G).
- To identify sites under positive selection within the IHNV G protein.
- To map these sites onto a 3D protein structure for functional insights.
Main Methods:
- Sequencing of a 303 nt segment (mid-G region) from 88 IHNV Idaho isolates.
- Bayesian phylogenetic analysis (MrBayes) to estimate positive selection at codon sites.
- 3D protein structure modeling using CPHmodels, with VSV glycoprotein as a template.
Main Results:
- Identified specific amino acid sites under positive selection in the IHNV G protein.
- Mapped these selected sites onto the predicted 3D structure.
- Selected sites are located on the protein surface, suggesting roles in antigen-antibody interactions.
Conclusions:
- Positively selected sites in IHNV G protein correlate with known mutation hotspots and antigenic sites.
- This knowledge enhances understanding of IHNV-host immune system interactions.
- Findings can inform vaccine development strategies for IHNV and other viral pathogens.
