PMID: 11315174Apr 21, 2001Paper

Schistosoma japonicum cathepsin D aspartic protease cleaves human IgG and other serum components

Parasitology
Christiana K VerityPaul J Brindley

Abstract

Recombinant cathepsin D aspartic protease of Schistosoma japonicum cleaved human IgG in vitro in a time and dose-dependent manner. Optimal cleavage was seen at pH 3.6-4.5; modest cleavage remained at pH 5.0, and no cleavage was detected above pH 5.0. Amino terminal sequencing of the major cleavage fragments of human IgG identified a Fab fragment from the VH1 domain, and 2 cleavage sites in the CH2 domain below the hinge region. The P1 and P1' residues at the 2 CH2 cleavage sites were Phe254-Leu255 and Leu325-Thr326, indicating a preference by the schistosome protease for bulky hydrophobic residues flanking the scissile bond. No cleavage of the immunoglobulin light chain was detected. In addition, the recombinant schistosome protease indiscriminately degraded the human serum proteins complement C3 and serum albumin into numerous small fragments. These results demonstrate specific cleavage of human IgG by the recombinant schistosome aspartic protease, and highlight the broad range digestive specificity of the enzyme which may play a role in the degradation of host serum proteins ingested as part of the schistosome bloodmeal.

Citations

Aug 8, 2002·Parasite Immunology·Christiana K VerityPaul J Brindley
Oct 5, 2001·Clinical Microbiology Reviews·A Loukas, P Prociv
Aug 19, 2006·Parasite Immunology·R S McIntoshR J Pleass
Apr 24, 2004·Trends in Parasitology·Conor R CaffreyMohammed Sajid
Apr 25, 2007·Molecular and Biochemical Parasitology·Melaine DelcroixJames H McKerrow
Jan 25, 2011·Experimental Parasitology·Leigh SchulteMalcolm K Jones
Dec 24, 2002·The Journal of Immunology : Official Journal of the American Association of Immunologists·Anne Camille La FlammeEdward J Pearce
Feb 23, 2021·Frontiers in Immunology·Jacob R Hambrook, Patrick C Hanington
Jul 11, 2006·Journal of Pharmaceutical and Biomedical Analysis·Lei YuBing He

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