Scabies mite inactivated serine protease paralogues are present both internally in the mite gut and externally in feces

C Willis, K FISCHER, S Walton,, Bart Currie, D KEMP

    Research output: Contribution to journalArticleResearchpeer-review

    Abstract

    The scabies mite, Sarcoptes scabiei, is the causative agent of scabies, a disease that is common among disadvantaged populations and facilitates streptococcal infections with serious sequelae. Previously, we encountered large families of genes encoding paralogues of house dust mite protease allergens with their catalytic sites inactivated by mutation (scabies mite inactivated protease paralogues [SMIPPs]). We postulated that SMIPPs have evolved as an adaptation to the parasitic lifestyle of the scabies mite, functioning as competitive inhibitors of proteases involved in the host-parasite interaction. To propose testable hypotheses for their functions, it is essential to know their locations in the mite. Here we show by immunohistochemistry that SMIPPs exist in two compartments: 1) internal to the mite in the gut and 2) external to the mite after excretion from the gut in scybala (fecal pellets). SMIPPs may well function in both of these compartments to evade host proteases. Copyright � 2006 by The American Society of Tropical Medicine and Hygiene.
    Original languageEnglish
    Pages (from-to)683-687
    Number of pages5
    JournalAmerican Journal of Tropical Medicine and Hygiene
    Volume75
    Issue number4
    Publication statusPublished - 2006

    Fingerprint

    Scabies
    Mites
    Serine Proteases
    Feces
    Peptide Hydrolases
    Sarcoptes scabiei
    Dermatophagoides Antigens
    Host-Parasite Interactions
    Streptococcal Infections
    Vulnerable Populations
    Protease Inhibitors
    Life Style
    Catalytic Domain
    Immunohistochemistry
    Mutation

    Cite this

    @article{a3c34140a4e04f70a71e8f35f5f8773f,
    title = "Scabies mite inactivated serine protease paralogues are present both internally in the mite gut and externally in feces",
    abstract = "The scabies mite, Sarcoptes scabiei, is the causative agent of scabies, a disease that is common among disadvantaged populations and facilitates streptococcal infections with serious sequelae. Previously, we encountered large families of genes encoding paralogues of house dust mite protease allergens with their catalytic sites inactivated by mutation (scabies mite inactivated protease paralogues [SMIPPs]). We postulated that SMIPPs have evolved as an adaptation to the parasitic lifestyle of the scabies mite, functioning as competitive inhibitors of proteases involved in the host-parasite interaction. To propose testable hypotheses for their functions, it is essential to know their locations in the mite. Here we show by immunohistochemistry that SMIPPs exist in two compartments: 1) internal to the mite in the gut and 2) external to the mite after excretion from the gut in scybala (fecal pellets). SMIPPs may well function in both of these compartments to evade host proteases. Copyright � 2006 by The American Society of Tropical Medicine and Hygiene.",
    keywords = "recombinant protein, serine proteinase, animal experiment, animal model, article, controlled study, enzyme inactivation, feces, host parasite interaction, human, human tissue, immunohistochemistry, intestine, mite, mouse, nonhuman, Sarcoptes scabiei, scabies, Streptococcus infection, animal, C57BL mouse, enzymology, immunology, parasitology, skin, Western blotting, Acari, Psoroptes cervinus, Pyroglyphidae, Animals, Blotting, Western, Feces, Host-Parasite Relations, Mice, Mice, Inbred C57BL, Scabies, Serine Endopeptidases, Skin",
    author = "C Willis and K FISCHER and S Walton, and Bart Currie and D KEMP",
    year = "2006",
    language = "English",
    volume = "75",
    pages = "683--687",
    journal = "The American Journal of Tropical Medicine and Hygiene",
    issn = "0002-9637",
    publisher = "American Society of Tropical Medicine and Hygiene",
    number = "4",

    }

    Scabies mite inactivated serine protease paralogues are present both internally in the mite gut and externally in feces. / Willis, C; FISCHER, K; Walton, S; Currie, Bart; KEMP, D.

    In: American Journal of Tropical Medicine and Hygiene, Vol. 75, No. 4, 2006, p. 683-687.

    Research output: Contribution to journalArticleResearchpeer-review

    TY - JOUR

    T1 - Scabies mite inactivated serine protease paralogues are present both internally in the mite gut and externally in feces

    AU - Willis, C

    AU - FISCHER, K

    AU - Walton,, S

    AU - Currie, Bart

    AU - KEMP, D

    PY - 2006

    Y1 - 2006

    N2 - The scabies mite, Sarcoptes scabiei, is the causative agent of scabies, a disease that is common among disadvantaged populations and facilitates streptococcal infections with serious sequelae. Previously, we encountered large families of genes encoding paralogues of house dust mite protease allergens with their catalytic sites inactivated by mutation (scabies mite inactivated protease paralogues [SMIPPs]). We postulated that SMIPPs have evolved as an adaptation to the parasitic lifestyle of the scabies mite, functioning as competitive inhibitors of proteases involved in the host-parasite interaction. To propose testable hypotheses for their functions, it is essential to know their locations in the mite. Here we show by immunohistochemistry that SMIPPs exist in two compartments: 1) internal to the mite in the gut and 2) external to the mite after excretion from the gut in scybala (fecal pellets). SMIPPs may well function in both of these compartments to evade host proteases. Copyright � 2006 by The American Society of Tropical Medicine and Hygiene.

    AB - The scabies mite, Sarcoptes scabiei, is the causative agent of scabies, a disease that is common among disadvantaged populations and facilitates streptococcal infections with serious sequelae. Previously, we encountered large families of genes encoding paralogues of house dust mite protease allergens with their catalytic sites inactivated by mutation (scabies mite inactivated protease paralogues [SMIPPs]). We postulated that SMIPPs have evolved as an adaptation to the parasitic lifestyle of the scabies mite, functioning as competitive inhibitors of proteases involved in the host-parasite interaction. To propose testable hypotheses for their functions, it is essential to know their locations in the mite. Here we show by immunohistochemistry that SMIPPs exist in two compartments: 1) internal to the mite in the gut and 2) external to the mite after excretion from the gut in scybala (fecal pellets). SMIPPs may well function in both of these compartments to evade host proteases. Copyright � 2006 by The American Society of Tropical Medicine and Hygiene.

    KW - recombinant protein

    KW - serine proteinase

    KW - animal experiment

    KW - animal model

    KW - article

    KW - controlled study

    KW - enzyme inactivation

    KW - feces

    KW - host parasite interaction

    KW - human

    KW - human tissue

    KW - immunohistochemistry

    KW - intestine

    KW - mite

    KW - mouse

    KW - nonhuman

    KW - Sarcoptes scabiei

    KW - scabies

    KW - Streptococcus infection

    KW - animal

    KW - C57BL mouse

    KW - enzymology

    KW - immunology

    KW - parasitology

    KW - skin

    KW - Western blotting

    KW - Acari

    KW - Psoroptes cervinus

    KW - Pyroglyphidae

    KW - Animals

    KW - Blotting, Western

    KW - Feces

    KW - Host-Parasite Relations

    KW - Mice

    KW - Mice, Inbred C57BL

    KW - Scabies

    KW - Serine Endopeptidases

    KW - Skin

    M3 - Article

    VL - 75

    SP - 683

    EP - 687

    JO - The American Journal of Tropical Medicine and Hygiene

    JF - The American Journal of Tropical Medicine and Hygiene

    SN - 0002-9637

    IS - 4

    ER -