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Predictive bioinformatic identification of minor receptor group human rhinoviruses
Author(s) -
Weber Christoph,
Pickl-Herk Angela,
Khan Abdul Ghafoor,
Strauss Sascha,
Carugo Oliviero,
Blaas Dieter
Publication year - 2009
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2009.07.015
Subject(s) - biology , capsid , ldl receptor , receptor , epitope , lysine , affinities , binding site , lipoprotein , virology , antibody , genetics , biochemistry , virus , amino acid , cholesterol
Major group HRVs bind intercellular adhesion molecule 1 and minor group HRVs bind members of the low‐density lipoprotein receptor (LDLR) family for cell entry. Whereas the former share common sequence motives in their viral capsid proteins (VPs), in the latter only a lysine residue within the binding epitope in VP1 is conserved; this lysine is also present in “K‐type” major group HRVs that fail to use LDLR for infection. By using the available sequences three‐dimensional models of VP1 of all HRVs were built and binding energies, with respect to module 3 of the very‐low‐density lipoprotein receptor, were calculated. Based on the predicted affinities K‐type HRVs and minor group HRVs were correctly classified.