Lack of Lysozyme Activity of Natural and Yeast-Derived Recombinant Der p 2

Hakkaart, G. A. J.; Aalberse, Rob C.; Ree, Ronald van

doi:10.1159/000237667

Cited by 9 publications

(7 citation statements)

References 7 publications

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“…At present, it is not clear whether this protein was responsible for the low specific lytic activity determined. We (this study) and others [37] failed to demonstrate activity with affinity‐purified Der p 2. The N‐terminal amino acid sequence of the protein in the phosphate fraction did not correspond to any protein in the data banks, and the sequence of the 1.0 M MgCl 2 ‐eluting fraction was not determined.…”

Section: Discussionmentioning

confidence: 44%

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

Pope

Lenzo

et al. 2002

FEMS Immunology &Amp; Medical Microbiology

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Bacteriolytic activity was detected in extracts of whole mite and spent growth medium (SGM) from the clinically important Dermatophagoides pteronyssinus and Dermatophagoides farinae mites and was most abundant in whole mite extract. Gram-positive organisms Micrococcus lysodeikticus, Bacillus megaterium and Listeria monocytogenes were preferentially lysed and the lytic activity was enhanced by thiols, destroyed by mite proteases, inhibited by HgCl2 and high concentrations of NaCl but was resistant to heat and acid treatment. Substrate SDS-PAGE analysis indicated the presence of several lytic enzymes, two of which were isolated from D. pteronyssinus spent growth medium extract by hydroxyapatite chromatography. The N-terminal amino acid sequence of one of them was then used in PCR-based cloning studies. The complete amino acid sequence of this protein was determined and cDNA found to encode a 130-amino acid residue mature protein with a 20-amino acid leader sequence. The deduced protein demonstrated sequence similarity with the C-terminal regions of a group of bacterial proteins belonging to the P60 superfamily. These data suggest that the enzyme is derived from bacteria within the mites rather than from mites per se.

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Section: Discussionmentioning

confidence: 44%

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

Pope

Lenzo

et al. 2002

FEMS Immunology &Amp; Medical Microbiology

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“…In the past, there had been a presumption that group 2 allergens are lysozymes, but it is now clear that they are not [ 28, 29]. The localization of major allergens in the dust mite Lepidoglyphus destructor has been reported [ 20], and it showed that the 15 kDa allergen, probably the group 2 allergen in L. destructor, was localized in the faecal pellets and gut lining.…”

Section: Discussionmentioning

confidence: 99%

Localization of a major allergen, Der p 2, in the gut and faecal pellets of Dermatophagoides pteronyssinus

Park

Lee

et al. 2000

Clin Experimental Allergy

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“…There was some speculation that Der p 2 may be a mite lysozyme, but it is clear that it is not [112], particularly now that the tertiary structure has been solved [113, 114]. Anti-group 2 antibodies have been reported to show reactivity associated with the gut and other unidentified structures [115, 116].…”

Section: Group 2 Allergensmentioning

confidence: 99%

“…Residues 47 and 114 are in adjacent loops and 111 is at the end of a β-strand while residue 40 is within a β strand. It is possible to distinguish the variants with monoclonal antibodies [112]and the residue 114 has been shown critical in this regard. The region of reactivity to the monoclonal antibodies was determined by hydrogen exchange and it corresponded to the cluster of sequence changes [131].…”

Section: Group 2 Allergensmentioning

confidence: 99%

Characterization and Immunobiology of House Dust Mite Allergens

Thomas¹,

Smith²,

Hales³

et al. 2002

Int Arch Allergy Immunol

303

254

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The examination of house dust mite extracts has indicated that over 30 different proteins can induce IgE antibody in patients allergic to the house dust mite. There are however dominant specificities especially the group 1 and 2 allergens which can account for much of the allergenicity of extracts. Of the 19 denominated allergens, the major IgE binding has been reported for the group 1, 2, 3, 9, 11, 14 and 15 allergens. The high-molecular-weight group 11, 14 and 15 allergens have only recently been described and although high IgE binding has been anticipated from immunoblotting, there is a need for considerable corroboration. Similarly, the study of the group 3 and 9 serine protease allergens has been incomplete. The group 4, 5, 7 and 8 allergens have shown intermediate IgE binding and the group 10 tropomyosins are of interest because of their potential cross-reactivity with allergen from disparate species. Although the progress with the production of recombinant group 1 allergens has been recent, many of the allergens can be produced as high IgE-binding polypeptides. The tertiary structure of the group 2 allergens has been determined from recombinant proteins and they are an excellent model for the investigation of modified allergens. An unexpected property of the group 1, 2 and 3 allergens has been the high degree of polymorphism found by cDNA analysis. It has however been possible to identify sequences to represent the variation in the natural allergens. The group 7 and 14 allergens show secondary modifications which vary in different extracts creating batch variation. While some estimate of the importance of allergens can be obtained from IgE binding, few analyses of T-cell responses have been made and these regulate both the development of, and the protection from sensitization.

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Lack of Lysozyme Activity of Natural and Yeast-Derived Recombinant Der p 2

Cited by 9 publications

References 7 publications

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

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

Localization of a major allergen, Der p 2, in the gut and faecal pellets of Dermatophagoides pteronyssinus

Characterization and Immunobiology of House Dust Mite Allergens

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