Minor group human rhinovirus-receptor interactions: geometry of multimodular attachment and basis of recognition.
X-ray structures of human rhinovirus 2 (HRV2) in complex with soluble very-low-density lipoprotein receptors encompassing modules 1, 2, and 3 (V123) and five V3 modules arranged in tandem (V33333) demonstrates multi-modular binding around the virion's five-fold axes. Occupancy was 60% for V123 and 100% for V33333 explaining the high-avidity of the interaction. Surface potentials of 3D-models of all minor group HRVs and K-type major group HRVs were compared; hydrophobic interactions between a conserved lysine in the viruses and a tryptophan in the receptor modules together with coulombic attraction via diffuse opposite surface potentials determine minor group HRV receptor specificity.
Querol-Audí
Jordi
J
Institut de Biologia Molecular de Barcelona (CSIC), Parc Científic de Barcelona, Barcelona, Spain.
Konecsni
Tuende
T
Pous
Joan
J
Carugo
Oliviero
O
Fita
Ignasi
I
Verdaguer
Nuria
N
Blaas
Dieter
D
D018360:Crystallography, X-Ray; D006801:Humans; D008958:Models, Molecular; D011487:Protein Conformation; D011973:Receptors, LDL / Q000737:chemistry* / Q000502:physiology; D011991:Receptors, Virus / Q000737:chemistry* / Q000502:physiology; D012229:Rhinovirus / Q000737:chemistry* / Q000502:physiology
D011973:Receptors, LDL; D011991:Receptors, Virus; C036053:VLDL receptor