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Published online before print March 27, 2008, 10.1110/ps.073366208
Protein Science (2008), 17:813-820. Published by Cold Spring Harbor Laboratory Press. Copyright © 2008 The Protein Society
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Structure and ion channel activity of the human respiratory syncytial virus (hRSV) small hydrophobic protein transmembrane domain

Siok Wan Gan, Lifang Ng, Xin Lin, Xiandi Gong, and Jaume Torres

School of Biological Sciences, Nanyang Technological University, 637551 Singapore

(RECEIVED November 22, 2007; FINAL REVISION January 21, 2008; ACCEPTED January 21, 2008)

The small hydrophobic (SH) protein from the human respiratory syncytial virus (hRSV) is a glycoprotein of ~64 amino acids with one putative {alpha}-helical transmembrane domain. Although SH protein is important for viral infectivity, its exact role during viral infection is not clear. Herein, we have studied the secondary structure, orientation, and oligomerization of the transmembrane domain of SH (SH-TM) in the presence of lipid bilayers. Only one oligomer, a pentamer, was observed in PFO-PAGE. Using polarized attenuated total reflection-Fourier transform infrared (PATR-FTIR) spectroscopy, we show that the SH-TM is {alpha}-helical. The rotational orientation of SH-TM was determined by site-specific infrared dichroism (SSID) at two consecutive isotopically labeled residues. This orientation is consistent with that of an evolutionary conserved pentameric model obtained from a global search protocol using 13 homologous sequences of RSV. Conductance studies of SH-TM indicate ion channel activity, which is cation selective, and inactive below the predicted pKa of histidine. Thus, our results provide experimental evidence that the transmembrane domain of SH protein forms pentameric {alpha}-helical bundles that form cation-selective ion channels in planar lipid bilayers. We provide a model for this pore, which should be useful in mutagenesis studies to elucidate its role during the virus cycle.

Keywords: small hydrophobic protein; ion channel; infrared dichroism; molecular dynamics


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K. Parthasarathy, L. Ng, X. Lin, D. X. Liu, K. Pervushin, X. Gong, and J. Torres
Structural Flexibility of the Pentameric SARS Coronavirus Envelope Protein Ion Channel
Biophys. J., September 15, 2008; 95(6): L39 - L41.
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