This Article Full Text Full Text (PDF) Other Versions of this Article: JVI.02664-07v1 82/14/7167    most recent Alert me when this article is cited Alert me if a correction is posted Services Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Reprints and Permissions Copyright Information Books from ASM Press MicrobeWorld Google Scholar Articles by Khan, S. Articles by Wimmer, E. PubMed PubMed Citation Articles by Khan, S. Articles by Wimmer, E.

 Previous Article  |  Next Article 

Journal of Virology, July 2008, p. 7167-7179, Vol. 82, No. 14
0022-538X/08/$08.00+0     doi:10.1128/JVI.02664-07
Copyright © 2008, American Society for Microbiology. All Rights Reserved.

Characterization of the New World Monkey Homologues of Human Poliovirus Receptor CD155

Shaukat Khan,¹ Xiaozhong Peng,^1, Jiang Yin,^1, Ping Zhang,² and Eckard Wimmer^1*

Department of Molecular Genetics and Microbiology, Stony Brook University, Stony Brook, New York 11794,¹ Department of Biological Sciences, Purdue University, West Lafayette, Indiana 47907²

Received 14 December 2007/ Accepted 5 May 2008

In contrast to Old World monkeys, most New World monkeys (NWMs) are not susceptible to poliovirus (PV), regardless of the route of infection. We have investigated the molecular basis of restricted PV pathogenesis of NWMs with two kidney cell lines of NWMs, TMX (tamarin) and NZP-60 (marmoset), and characterized their PV receptor homologues. TMX cells were susceptible to infection by PV1 (Mahoney) and PV3 (Leon) but not by PV2 (Lansing). Binding studies to TMX cells indicated that the formation of PV/receptor complexes increased when measured first at 4°C and then at 25°C, whereas PV2 did not significantly bind to TMX cells at either temperature. On the other hand, NZP-60 cells were not susceptible to infection by any of the PV serotypes. However, a low amount of PV1 bound to NZP-60 cells at 4°C, but there was no increase of binding at 25°C. In contrast, both NWM cell lines supported genome replication and virion formation when transfected with viral RNAs of either serotype, an observation indicating that infection was blocked in receptor-virus interaction. To overcome the receptor block, we substituted 3 amino acids in the marmoset receptor (nCD155), H80Q, N85S, and P87S, found in the human PV receptor, hCD155. Cells expressing the mutant receptor (L-nCD155mt) were now susceptible to infection with PV1, which correlated with an increase in PV1-bound receptor complexes from 4°C to 25°C. L-nCD155mt cells were, however, still resistant to PV2 and PV3. These data show that an increase in the formation of PV/receptor complexes, when measured at 4°C and at 25°C, correlates with and is an indicator of successful infection at 37°C, suggesting that the complex formed at 25°C may be an intermediate in PV uptake.

Published ahead of print on 14 May 2008.

Present address: The National Laboratory of Medical Molecular Biology, Institute of Basic Medical Sciences, Chinese Academy of Medical Sciences and Peking Union Medical College, Beijing, China.

Present address: Department of Biochemistry, University of Alberta, Edmonton, Alberta, Canada T6G 2H7.