HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS		QUICK SEARCH:   [advanced] Author: Keyword(s): Year:  Vol:  Page:

This Article Full Text Full Text (PDF) Alert me when this article is cited Alert me if a correction is posted Citation Map Services Email this article to a friend Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Citing Articles Citing Articles via HighWire Citing Articles via CrossRef Citing Articles via Google Scholar Google Scholar Articles by García-Barreno, B. Articles by Melero, J. A. Search for Related Content PubMed PubMed Citation Articles by García-Barreno, B. Articles by Melero, J. A. Agricola Articles by García-Barreno, B. Articles by Melero, J. A.

Epitope mapping of human respiratory syncytial virus 22K transcription antitermination factor: role of N-terminal sequences in protein folding

¹ Centro Nacional de Microbiología, Instituto de Salud Carlos III, Majadahonda, 28220 Madrid, Spain
² MRC Virology Unit, Institute for Virology, Church Street, Glasgow G11 5JR, UK
³ The Centre for Infectious Diseases, Wolfson Institute, University of Durham, Queen's Campus, Stockton-on-Tees TS17 6BH, UK

Correspondence
José A. Melero
jmelero{at}isciii.es

The reactivity of a panel of 12 monoclonal antibodies raised against the human respiratory syncytial virus 22 kDa (22K) protein was tested by Western blotting with a set of 22K deletion mutants. The results obtained identified sequences in the C-terminal half of the 22K polypeptide required for integrity of most antibody epitopes, except for epitope 112, which was lost in mutants with short N-terminal deletions. This antibody, in contrast to the others, failed to immunoprecipitate the native 22K protein, indicating that the N terminus of this protein is buried in the native molecule and exposed only under the denaturing conditions of Western blotting. In addition, N-terminal deletions that abolished reactivity with monoclonal antibody 112 also inhibited phosphorylation of the 22K protein previously identified at Ser-58 and Ser-61, suggesting that the N terminus is important in regulating the 22K protein phosphorylation status, most likely as a result of its requirement for protein folding.

This article has been cited by other articles:

				V. M. Cowton, D. R. McGivern, and R. Fearns Unravelling the complexities of respiratory syncytial virus RNA synthesis J. Gen. Virol., July 1, 2006; 87(7): 1805 - 1821. [Abstract] [Full Text] [PDF]