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

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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

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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.",
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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",
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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 -