PCR Detection of the 14.5 Antibacterial NlpC/P60-Like <I>Dermatophagoides pteronyssinus</I> Protein in <I>Dermatophagoides farinae</I> (Acari: Pyroglyphidae)

Abstract

House dust mites produce antibacterial proteins suppressing bacterial growth. The 14.5-kDa bacteriolytic protein (UniProtKB Q8MWR6) has been known in Dermatophagoides pteronyssinus Trouessart. We have applied polymerase chain reaction and reverse transcription-PCR to detect a homologous gene sequence coding for a Q8MWR6-related protein in Dermatophagoides farinae (Hughes) using genomic DNA and total RNA, respectively. The resulting PCR product of expected size, 243 bp, was obtained from both Dermatophagoides spp., while no amplification was achieved from stored product mite samples. Sequence of the gene fragment from D. farinae showed 83% similarity to the previously described one in D. pteronyssinus. Successful amplification of the expected product from cDNA generated with oligo-dT primer implies that the NlpC/P60-like protein in Dermatophagoides mites is of eukaryotic or mite origin.

Comparative Genomics Reveals Insights into the Divergent Evolution of Astigmatic Mites and Household Pest Adaptations

“…S12 C , Supplementary Material online). This peptidoglycan endopeptidase has been reported and explored in several astigmatic mites ( Mathaba et al 2002 ; Erban et al 2013 ; Chan et al 2015 ; Tang et al 2015 , 2017 ).…”

“…In astigmatic mites, except for the HGT peptidoglycan endopeptidase, which was identified and explored ( Mathaba et al 2002 ; Erban et al 2013 ; Chan et al 2015 ; Tang et al 2015 , 2017 ), very few HGT events were reported previously. UGTs, chitinases, and other genes were reported as HGT genes in spider mites ( Ahn et al 2014 ; Wybouw et al 2018 ; Snoeck et al 2019 ).…”

House dust mites possess a polymorphic, single domain putative peptidoglycan d,l endopeptidase belonging to the NlpC/P60 Superfamily

“…The percent GC contents of the nucleotide sequences were 38.9, 39.3, 38.5, 36.7, 41.9 and 58, for lytFM , lytFM1 , lytFM2 , D. farinae , P. ovis and B. tropicalis homologues, respectively. Two conservative polymorphisms were detected when the full‐length [19] and partial [26] D. farinae sequences were compared, namely Lys for Arg at residue position 29 and Ile for Leu at position 45 (mature D. pteronyssinus numbering, Fig. 2).…”

Comparative Genomics Reveals Insights into the Divergent Evolution of Astigmatic Mites and Household Pest Adaptations

“…6 and Table S31). Except the peptidoglycan endopeptidase reported in both D. farinae and D. pteronyssinus [46][47][48] , none of other HGT events was reported in astigmatic mites previously. UGTs, chitinase and other genes were reported as HGT genes in spider mite [58][59][60] .…”

“…We also found that the peptidoglycan endopeptidase was tandemly duplicated in both P. ovis and T. putrescentiae, while decayed (complete deletion) in S. scabiei. This peptidoglycan endopeptidase was reported in both D. farinae and D. pteronyssinus [46][47][48] . These HGT-gained lytic enzymes for fungal and bacterial cell wall are considered to play vital roles in the digestive functions of astigmatic mites, particularly house dust mites, D. farinae and D. pteronyssinus feeding on human skin flakes colonized by microbes including fungi and bacteria 10,49,50 .…”