Isolation and characterisation of a 13.8-kDa bacteriolytic enzyme from house dust mite extracts: homology with prokaryotic proteins suggests that the enzyme could be bacterially derived

Mathaba, L

doi:10.1016/s0928-8244(02)00280-8

Cited by 6 publications

(24 citation statements)

References 43 publications

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“…In house dust mites, Dermatophagoides pteronyssinus and D. farinae, lysozyme activity has been reported in both whole mite extracts (WME) and spent growth medium extracts (SGME), i.e., an extract of the medium after mite cultivation, containing faeces and debris of the rearing diet without mites (Childs and Bowman 1981;Mathaba et al 2002;Stewart et al 1998). It was suggested that group 2 mite allergens of D. pteronyssinus displayed lysozyme activity, but the Der p2 lacked lysozyme activity (Hakkaart et al 1997).…”

Section: Introductionmentioning

confidence: 99%

Digestive function of lysozyme in synanthropic acaridid mites enables utilization of bacteria as a food source

Erban

Hubert

2008

Exp Appl Acarol

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The activity of lysozyme, the enzyme that hydrolyzes peptidoglycan in G(+) bacterial cell walls, was detected in whole mite extracts (WME) and in spent growth medium extracts (SGME) of 14 species of synanthropic mites (Acari: Acaridida). The adaptation of lysozyme for digestive activity and bacteriophagy was based on: (i) high lysozyme activity in SGME, and (ii) the correlation of maximum lysozyme activity at acidic pH values, corresponding to pH in the ventriculus and caeca. We show that the digestion of fluorescein-labeled Micrococcus lysodeikticus cells began in ventriculus and continued during the passage of a food bolus through the gut. The fluorescein was absorbed by midgut cells and penetrated to parenchymal tissues. Eight species showed a higher rate of population growth on a M. lysodeikticus diet than on a control diet. The lysozyme activity in SGME was positively correlated to the standardized rate (r (s)) of population growth, although no correlation was found between r (s) and lysozyme activity in WME. The lysozyme activity in WME was negatively correlated to that in SGME. The highest activity of digestive lysozyme was found in Lepidoglyphus destructor, Chortoglyphus arcuatus and Dermatophagoides farinae. All of these findings indicate that lysozyme in acaridid mites possesses both defensive and digestive functions. The enzymatic properties of mite lysozyme are similar to those of the lysozymes present in the ruminant stomach and in the insect midgut.

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Section: Introductionmentioning

confidence: 99%

Digestive function of lysozyme in synanthropic acaridid mites enables utilization of bacteria as a food source

Erban

Hubert

2008

Exp Appl Acarol

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“…2. Alignment of a partial sequence of 14.5-kDa bacteriolytic enzyme in D. pteronyssinus (Mathaba et al 2002), with deduced amino-acid sequences of the gene fragment retrieved from D. farinae (this work), and corresponding parts of the closest homologs found in bacteria (Streptomyces sp., Mycobacterium sp., Gordonia effusa) and fungi (Aspergillus terreus, Metarhizium anisopliae, Beauveria bassiana, and Cordyceps militaris). Numbering according to the D. pteronyssinus protein.…”

Section: Resultsmentioning

confidence: 99%

“…Although the protein showed bacteriolytic activity and molecular mass similar to lysozymes, the sequence analysis indicated similarity to prokaryotic P60 proteins (Mathaba et al 2002). In the current study, we identiÞed a homologous protein in D. farinae.…”

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confidence: 98%

“…Recently, the bacterial adjuvant compounds from the house dust mites as well as intrinsic biological properties of house dust mite allergens are suggested as determining factors for the stimulation of innate immune systems (Jacquet 2011). Mathaba et al (2002) suggested that Dermatophagoides pteronyssinus (Trouessart 1897) possess several bacteriolytic enzymes. The bacteriolytic enzymes can correspond to the digestive lysozymes present in astigmatid mites including D. pteronyssinus and Dermatophagoides farinae Hughes 1961 (Childs andBowman 1981, Erban andHubert 2008).…”

mentioning

confidence: 99%

“…The bacteriolytic enzymes can correspond to the digestive lysozymes present in astigmatid mites including D. pteronyssinus and Dermatophagoides farinae Hughes 1961 (Childs andBowman 1981, Erban andHubert 2008). Mathaba et al (2002) puriÞed and analyzed a 13.8-kDa protein (14.5 kDa according to deduced amino acid sequence; UniProtKB Q8MWR6) from the faeces fraction (SGME) of D. pteronyssinus.…”

mentioning

confidence: 99%

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

Erban

Presa²,

Kopecký

et al. 2013

jnl. med. entom.

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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.

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Dermatophagoides pteronyssinus lytFM encoding an NlpC/P60 endopeptidase is also present in mite‐associated bacteria that express LytFM variants

2017

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The bodies and faecal pellets of the house dust mite ( HDM ), Dermatophagoides pteronyssinus , are the source of many allergenic and nonallergenic proteins. One of these, the 14‐ kD a bacteriolytic enzyme Lyt FM , originally isolated from the spent HDM growth medium, may contribute to bacteriolytic activity previously detected by zymography at 14 kD a in the culture supernatants of some bacterial species isolated from surface‐sterilised HDM . Based on previously reported findings of lateral gene transfer between microbes and their eukaryotic hosts, we investigated the presence of lyt FM in the genomes of nine Gram‐positive bacteria from surface‐sterilised HDM , and the expression by these isolates of Lyt FM and its variants Lyt FM 1/Lyt FM 2. The lyt FM gene was detected by PCR in the genomes of three of the isolates: Bacillus licheniformis strain 1, B. licheniformis strain 2 and Staphylococcus aureus . Expression of the variant Lyt FM 1 was detected in culture supernatants of these bacteria by mass spectrometry ( MS ) and ELISA , and the bacterial Lyt FM proteins were shown by zymography to be able to hydrolyse peptidoglycan. Our previous reports of Lyt FM homologues in other mite species and their phylogenetic analysis had suggested that they originated from a common mite ancestor. The phylogenetic analysis reported herein and the detection of other D. pteronyssinus proteins by MS in the culture supernatants of the three isolates that secreted Lyt FM 1 further support the hypothesis of lateral gene transfer to the bacterial endosymbionts from their HDM host. The complete sequence homology observed between the genes amplified from the microbes and those in their eukaryotic host indicated that the lateral gene transfer was an event that occurred recently.

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Isolation and characterisation of a 13.8-kDa bacteriolytic enzyme from house dust mite extracts: homology with prokaryotic proteins suggests that the enzyme could be bacterially derived

Cited by 6 publications

References 43 publications

Digestive function of lysozyme in synanthropic acaridid mites enables utilization of bacteria as a food source

Digestive function of lysozyme in synanthropic acaridid mites enables utilization of bacteria as a food source

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

Dermatophagoides pteronyssinus lytFM encoding an NlpC/P60 endopeptidase is also present in mite‐associated bacteria that express LytFM variants

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