Date of Award
Spring 4-24-2013
Degree Type
Thesis
Degree Name
Master of Science (MS)
Department
Biology
First Advisor
Dr. Roberta Attanasio
Second Advisor
Dr. Robert Harrison
Third Advisor
Dr. Franco Scinicariello
Abstract
Rhesus macaques are a widely used animal model of human diseases and related immune responses. Fc receptors (FcRs) mediate the interaction between antibody molecules and innate killing mechanisms, consequently eliminating the pathogen. In rhesus macaques, FcRs are highly polymorphic. To evaluate the potential influence of FcgR polymorphisms on the interaction with antibody molecules, we performed in silico analysis using SIFT, Provean, nsSNPAnalyzer, I-Mutant, MuSTAB and iPTREE-STAB web servers. V20G in FcγRI, I137K in FcγRII and I233V in FcγRIII were further analyzed structurally using FOLD-X, AMMP and Chimera to calculate changes in folding and interaction energy and for structure visualization. Results from our analysis suggest that the selected variations destabilize protein structure. Additionally, Q32R increases the binding affinity of FcγRI, whereas A131T decreases the binding affinity of FcγRII towards IgG1. Together, our results indicate that these substitutions might influence effector and regulatory mechanisms resulting from antibody/FcR interactions.
DOI
https://doi.org/10.57709/4111311
Recommended Citation
Sanghvi, Rashesh, "In Silico Analysis Shows That Single Aminoacid Variations In Rhesus Macacque Fcγreceptor Affect Protein Stability And Binding Affinity To IgG1." Thesis, Georgia State University, 2013.
doi: https://doi.org/10.57709/4111311