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) Supplementary figure 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 Hope, R. G. Articles by McLauchlan, J. Search for Related Content PubMed PubMed Citation Articles by Hope, R. G. Articles by McLauchlan, J. Agricola Articles by Hope, R. G. Articles by McLauchlan, J.

Efficient cleavage by signal peptide peptidase requires residues within the signal peptide between the core and E1 proteins of hepatitis C virus strain J1

MRC Virology Unit, Institute of Virology, Church Street, Glasgow G11 5JR, UK

Correspondence
John McLauchlan
j.mclauchlan{at}vir.gla.ac.uk

Maturation of hepatitis C virus (HCV) core protein requires cleavage by signal peptidase (SP) and signal peptide peptidase (SPP) at a signal peptide between core and the E1 glycoprotein. For HCV strain Glasgow, amino acids Ala¹⁸⁰, Ser¹⁸³ and Cys¹⁸⁴ within the signal peptide have previously been shown to be essential for efficient SPP cleavage. By contrast, these residues apparently did not contribute to core maturation in HCV strain J1. In the present study, the source of this discrepancy has been analysed and it is concluded that interpretation of the strain J1 data was incorrect, due to the inability to separate wild-type and mutant forms of core on gels by using standard buffer systems.

A supplementary figure showing the stability of core_wt and core_ASC/VLV proteins that lack aa 125–144 is available in JGV Online.

This article has been cited by other articles:

				K. Okamoto, Y. Mori, Y. Komoda, T. Okamoto, M. Okochi, M. Takeda, T. Suzuki, K. Moriishi, and Y. Matsuura Intramembrane Processing by Signal Peptide Peptidase Regulates the Membrane Localization of Hepatitis C Virus Core Protein and Viral Propagation J. Virol., September 1, 2008; 82(17): 8349 - 8361. [Abstract] [Full Text] [PDF]

				P. Targett-Adams, G. Hope, S. Boulant, and J. McLauchlan Maturation of Hepatitis C Virus Core Protein by Signal Peptide Peptidase Is Required for Virus Production J. Biol. Chem., June 13, 2008; 283(24): 16850 - 16859. [Abstract] [Full Text] [PDF]

				C. L. Murray, C. T. Jones, J. Tassello, and C. M. Rice Alanine Scanning of the Hepatitis C Virus Core Protein Reveals Numerous Residues Essential for Production of Infectious Virus J. Virol., October 1, 2007; 81(19): 10220 - 10231. [Abstract] [Full Text] [PDF]

				C Hourioux, R Patient, A Morin, E Blanchard, A Moreau, S Trassard, B Giraudeau, and P Roingeard The genotype 3-specific hepatitis C virus core protein residue phenylalanine 164 increases steatosis in an in vitro cellular model Gut, September 1, 2007; 56(9): 1302 - 1308. [Abstract] [Full Text] [PDF]

				S. Boulant, P. Targett-Adams, and J. McLauchlan Disrupting the association of hepatitis C virus core protein with lipid droplets correlates with a loss in production of infectious virus J. Gen. Virol., August 1, 2007; 88(8): 2204 - 2213. [Abstract] [Full Text] [PDF]

				P. Targett-Adams, T. Schaller, G. Hope, R. E. Lanford, S. M. Lemon, A. Martin, and J. McLauchlan Signal Peptide Peptidase Cleavage of GB Virus B Core Protein Is Required for Productive Infection in Vivo J. Biol. Chem., September 29, 2006; 281(39): 29221 - 29227. [Abstract] [Full Text] [PDF]