TY - JOUR
T1 - Interactions of decay-accelerating factor (DAF) with haemagglutinating human enteroviruses: utilizing variation in primate DAF to map virus binding sites
AU - Williams, DT
AU - Chaudhry, Y
AU - Goodfellow, IG
AU - Lea, S
AU - Evans, DJ
PY - 2004/3
Y1 - 2004/3
N2 - A cellular receptor for the haemagglutinating enteroviruses (HEV), and the protein that mediates haemagglutination, is the membrane complement regulatory protein decay accelerating factor (DAF; CD55). Although primate DAF is highly conserved, significant differences exist to enable cell lines derived from primates to be utilized for the characterization of the DAF binding phenotype of human enteroviruses. Thus, several distinct DAF-binding phenotypes of a selection of HEVS (viz. coxsackievirus A21 and echoviruses 6, 7, 11 -13, 29) were identified from binding and infection assays using a panel of primate cells derived from human, orang-utan, African Green monkey and baboon tissues. These studies complement our recent determination of the crystal structure of SCR34 of human DAF [Williams, P., Chaudhry, Y., Goodfellow, 1. G., Billington, J., Powell, R., Spiller, O. B., Evans, D. J. & Lea, S. (2003). J Biol Chem 278, 10691-10696] and have enabled us to better map the regions of DAF with which enteroviruses interact and, in certain cases, predict specific virus-receptor contacts.
AB - A cellular receptor for the haemagglutinating enteroviruses (HEV), and the protein that mediates haemagglutination, is the membrane complement regulatory protein decay accelerating factor (DAF; CD55). Although primate DAF is highly conserved, significant differences exist to enable cell lines derived from primates to be utilized for the characterization of the DAF binding phenotype of human enteroviruses. Thus, several distinct DAF-binding phenotypes of a selection of HEVS (viz. coxsackievirus A21 and echoviruses 6, 7, 11 -13, 29) were identified from binding and infection assays using a panel of primate cells derived from human, orang-utan, African Green monkey and baboon tissues. These studies complement our recent determination of the crystal structure of SCR34 of human DAF [Williams, P., Chaudhry, Y., Goodfellow, 1. G., Billington, J., Powell, R., Spiller, O. B., Evans, D. J. & Lea, S. (2003). J Biol Chem 278, 10691-10696] and have enabled us to better map the regions of DAF with which enteroviruses interact and, in certain cases, predict specific virus-receptor contacts.
KW - TRANSMEMBRANE RECEPTOR CD97
KW - COXSACKIE-B VIRUSES
KW - FACTOR CD55
KW - CELL ATTACHMENT
KW - ECHOVIRUS-7
KW - DOMAINS
KW - INFECTION
KW - REQUIRES
KW - PROTEIN
U2 - 10.1099/vir.0.19674-0
DO - 10.1099/vir.0.19674-0
M3 - Article
SN - 0022-1317
VL - 85
SP - 731
EP - 738
JO - Journal of General Virology
JF - Journal of General Virology
ER -