Function of the Respiratory Syncytial Virus Small Hydrophobic Protein
نویسندگان
چکیده
منابع مشابه
The small hydrophobic protein of the human respiratory syncytial virus forms pentameric ion channels.
The small hydrophobic (SH) protein is encoded by the human respiratory syncytial virus. Its absence leads to viral attenuation in the context of whole organisms, and it prevents apoptosis in infected cells. Herein, we have examined the structure of SH protein in detergent micelles and in lipid bilayers, by solution NMR and attenuated total reflection-Fourier transform infrared spectroscopy, res...
متن کاملStructural and Functional Aspects of the Small Hydrophobic (SH) Protein in the Human Respiratory Syncytial Virus
hRSV is the leading cause of respiratory disease in infants, elderly, and immunocompromised populations worldwide (Falsey et al., 2005; Nair et al., 2010). Most individuals are infected at a young age, before 3 years old (Glezen et al., 1986). In fact, RSV infection is the most common cause of hospitalization in children 5 years old and below. When severe infection occurs, respiratory airways a...
متن کاملMembrane orientation and oligomerization of the small hydrophobic protein of human respiratory syncytial virus.
Previous work has demonstrated that the small hydrophobic (SH) protein of human respiratory syncytial virus (RSV) A2 strain is a 64 amino acid integral membrane protein that accumulates intracellularly as an unglycosylated major species (SH0), a minor species truncated at the amino terminus and two N-glycosylated species one of which contains a further addition of polylactosamine. In this study...
متن کاملThe small hydrophobic protein of human respiratory syncytial virus: comparison between antigenic subgroups A and B.
The nucleotide and amino acid sequences of the mRNA and predicted polypeptide of the integral membrane small hydrophobic (SH) protein of human respiratory syncytial virus strain 18537 (a prototype strain of antigenic subgroup B) were determined from cloned cDNA. At the nucleotide and amino acid levels there was 78% and 76% identity, respectively, with the previously described SH mRNA and protei...
متن کاملModeling the structure of the respiratory syncytial virus small hydrophobic protein by silent-mutation analysis of global searching molecular dynamics.
Human respiratory syncytial virus (RSV) encodes a small hydrophobic (SH) protein, whose function in the life cycle of the virus is unknown. Recent channel activity measurements of the protein suggest that like other viroporins, SH may assemble into a homo-oligomeric ion channel. To further our understanding of this potentially important protein, a new strategy was implemented in order to model ...
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ژورنال
عنوان ژورنال: Journal of Virology
سال: 2007
ISSN: 0022-538X,1098-5514
DOI: 10.1128/jvi.02717-06