Expression of the Cydia pomonella granulovirus matrix metalloprotease enhances Autographa californica multiple nucleopolyhedrovirus virulence and can partially substitute for viral cathepsin

Virology
Egide IshimweA Lorena Passarelli

Abstract

The Cydia pomonella granulovirus open reading frame 46 (CpGV-ORF46) contains predicted domains found in matrix metalloproteases (MMPs), a family of zinc-dependent endopeptidases that degrade extracellular matrix proteins. We showed that CpGV-MMP was active in vitro. Autographa californica multiple nucleopolyhedrovirus (AcMNPV) expressing CpGV-ORF46 replicated similarly to a control virus lacking CpGV-ORF46 in cultured cells. The effects of AcMNPV expressing CpGV-MMP on virus infection in cultured cells and Trichoplusia ni larvae in the presence or absence of other viral degradative enzymes, cathepsin and chitinase, were evaluated. In the absence of cathepsin and chitinase or cathepsin alone, larval time of death was significantly delayed. This delay was compensated by the expression of CpGV-MMP. CpGV-MMP was also able to promote larvae melanization in the absence of cathepsin and chitinase. In addition, CpGV-MMP partially substituted for cathepsin in larvae liquefaction when chitinase, which is usually retained in the endoplasmic reticulum, was engineered to be secreted.

References

Jul 1, 1990·Proceedings of the National Academy of Sciences of the United States of America·H E Van Wart, H Birkedal-Hansen
Sep 6, 1994·Annals of the New York Academy of Sciences·R E GalardyB Summers
Apr 1, 1993·The Journal of General Virology·M M van OersJ M Vlak
Nov 27, 1999·The Journal of Biological Chemistry·J M MaidmentI M Clark
Sep 20, 2001·The Journal of General Virology·T LuqueD Winstanley
Aug 21, 2002·Journal of Virology·Erin A Crouch, A Lorena Passarelli
Nov 12, 2003·The Journal of Experimental Biology·Hans Merzendorfer, Lars Zimoch
Jun 18, 2004·Immunological Reviews·Lage Cerenius, Kenneth Söderhäll
Oct 19, 2004·Journal of Virological Methods·Stephen A KabaMonique M van Oers
Sep 24, 2005·Clinical and Experimental Immunology·P T G ElkingtonJ S Friedland
May 17, 2006·Biochemical and Biophysical Research Communications·Takaaki DaimonToru Shimada
Feb 24, 2007·Nature Reviews. Molecular Cell Biology·Andrea Page-McCawZena Werb
Jun 9, 2007·Archives of Virology·T DaimonT Shimada
Aug 19, 2007·The Journal of General Virology·Jeffrey J HodgsonPeter J Krell
Oct 16, 2007·Applied and Environmental Microbiology·Kiara G HeldCarleen M Collins
Jul 8, 2008·Journal of Virological Methods·Sally HiltonDoreen Winstanley
Jul 17, 2008·The Journal of Biological Chemistry·Hongnan KanBok Luel Lee
Dec 3, 2010·Journal of Cell Science·Christian FrantzValerie M Weaver
Nov 5, 2011·Nucleic Acids Research·Ivica LetunicPeer Bork
May 29, 2013·Biochimica Et Biophysica Acta·Thomas A Lagace, Neale D Ridgway
Jul 16, 2013·Virus Genes·George F RohrmannDavid A Theilmann
Oct 18, 2013·Molecular Biology and Evolution·Koichiro TamuraSudhir Kumar
Jan 13, 2015·The Journal of General Virology·Daniel M P Ardisson-AraujoRollie J Clem

❮ Previous
Next ❯

Citations

Feb 6, 2016·BMC Genomics·Daniel M P Ardisson-AraújoJosé L C Wolff
Dec 1, 2018·Archives of Virology·Aydın YesilyurtRemziye Nalcacioglu
Apr 11, 2017·Biochimica Et Biophysica Acta. Molecular Cell Research·Laura Marino-PuertasF Xavier Gomis-Rüth

❮ Previous
Next ❯

Related Concepts

Related Feeds

Aminoglycosides

Aminoglycoside is a medicinal and bacteriologic category of traditional Gram-negative antibacterial medications that inhibit protein synthesis and contain as a portion of the molecule an amino-modified glycoside. Discover the latest research on aminoglycoside here.

Aminoglycosides (ASM)

Aminoglycoside is a medicinal and bacteriologic category of traditional Gram-negative antibacterial medications that inhibit protein synthesis and contain as a portion of the molecule an amino-modified glycoside. Discover the latest research on aminoglycoside here.