Modeling of the Human Rhinovirus C Capsid Suggests a Novel Topography with Insights on Receptor Preference and Immunogenicity
| Autor: | Holly A. Basta, Jean-Yves Sgro, Ann C. Palmenberg |
|---|---|
| Jazyk: | angličtina |
| Rok vydání: | 2013 |
| Předmět: |
Rhinovirus C
Models Molecular Rhinovirus viruses Molecular Sequence Data Biology medicine.disease_cause Epitope Article 03 medical and health sciences Viral Proteins Immune system Capsid Species Specificity Virology medicine Humans Amino Acid Sequence Receptor Peptide sequence 030304 developmental biology Immune Evasion Genetics 0303 health sciences Picornaviridae Infections I-Tasser Immunogenicity 030302 biochemistry & molecular biology MODELLER biochemical phenomena metabolism and nutrition Intercellular Adhesion Molecule-1 3. Good health Capsid structure Receptors LDL Receptors Virus Receptor binding Model |
| Popis: | Features of human rhinovirus (RV)-C virions that allow them to use novel cell receptors and evade immune responses are unknown. Unlike the RV-A+B, these isolates cannot be propagated in typical culture systems or grown for structure studies. Comparative sequencing, I-TASSER, MODELLER, ROBETTA, and refined alignment techniques led to a structural approximation for C15 virions, based on the extensive, resolved RV-A+B datasets. The model predicts that all RV-C VP1 proteins are shorter by 21 residues relative to the RV-A, and 35 residues relative to the RV-B, effectively shaving the RV 5-fold plateau from the particle. There are major alterations in VP1 neutralizing epitopes and the structural determinants for ICAM-1 and LDLR receptors. The VP2 and VP3 elements are similar among all RV, but the loss of sequence “words” contributing Nim1ab has increased the apparent selective pressure among the RV-C to fix mutations elsewhere in the VP1, creating a possible compensatory epitope. |
| Databáze: | OpenAIRE |
| Externí odkaz: |
|