Open AccessHouse dust mites possess a polymorphic, single domain putative peptidoglycan d , l endopeptidase belonging to the NlpC/P60 Superfamily
Author(s) -
Tang Vivian H.,
Stewart Geoffrey A.,
Chang Barbara J.
Publication year - 2015
Publication title -
febs open bio
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.718
H-Index - 31
ISSN - 2211-5463
DOI - 10.1016/j.fob.2015.09.004
Subject(s) - biology , peptidoglycan , gene , microbiology and biotechnology , homology (biology) , genetics , endopeptidase , biochemistry , enzyme
A 14 kDa protein homologous to the γ‐ d ‐glutamyl‐ l ‐diamino acid endopeptidase members of the NlpC/P60 Superfamily has been described in Dermatophagoides pteronyssinus and Dermatophagoides farinae but it is not clear whether other species produce homologues. Bioinformatics revealed homologous genes in other Sarcopteformes mite species ( Psoroptes ovis and Blomia tropicalis ) but not in Tetranychus urticae and Metaseiulus occidentalis . The degrees of identity (similarity) between the D. pteronyssinus mature protein and those from D. farinae , P. ovis and B. tropicalis were 82% (96%), 77% (93%) and 61% (82%), respectively. Phylogenetic studies showed the mite proteins were monophyletic and shared a common ancestor with both actinomycetes and ascomycetes. The gene encoding the D. pteronyssinus protein was polymorphic and intronless in contrast to that reported for D. farinae . Homology studies suggest that the mite, ascomycete and actinomycete proteins are involved in the catalysis of stem peptide attached to peptidoglycan. The finding of a gene encoding a P60 family member in the D. pteronyssinus genome together with the presence of a bacterial promotor suggests an evolutionary link to one or more prokaryotic endosymbionts.