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Molecular analysis of Sarcoptes scabiei

Ljunggren, Erland L. (2005). Molecular analysis of Sarcoptes scabiei. Diss. (sammanfattning/summary) Uppsala : Sveriges lantbruksuniv., Acta Universitatis agriculturae Sueciae, 1652-6880 ; 2005:47
ISBN 91-576-7046-3
[Doctoral thesis]

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Abstract

The mite Sarcoptes scabiei (Acari), causes sarcoptic mange or scabies that globally affects animals and humans. Although scabies and mange are recognised as important diseases in human and veterinary medicine the amount of molecular studies of S. scabiei have been limited, which has been attributed to a shortage of parasitic material. This thesis is based on four studies that make use of molecular techniques with the aims to overcome the problems associated with a scarcity of mites, gain insights into the genetic background of the mite and to identify proteins important for host-parasite interactions. A better knowledge of parasite proteins that interact with the host is pivotal for understanding the mite’s pathogenicity. In order to accelerate gene discovery in S. scabiei an expressed sequence tag (EST) analysis of 1,020 ESTs was performed. Around half of the ESTs could be assigned with a putative gene identity. In the data set several proteases and allergens were identified, all of which possibly are involved in host-parasite interactions. The EST analysis identified a transcript corresponding to the enzyme gluthathione-S-transerase (GST). GST has an active role in detoxification, and has been a target molecule for vaccine development and drug resistance in other parasitic diseases. A phylogentic study showed that it was a delta-class GST, which previously never had been described in the order Acari. Several recombinant versions of the delta-GST were expressed and all were enzymatically active. Paramyosin, major Sarcoptes antigen 1 (MSA1) and atypical Sarcoptes antigen 1 (ASA1), were identified by immunoscreening, and later expressed as recombinant proteins for further characterisation. Paramyosin is an invertebrate muscle protein, associated with protective immunity in helminth infections. Sera from both dogs and pigs infected with S. scabiei reacted with recombinant paramyosin. ASA1 contained a MADF domain, which is not normally associated with antigens. In a Western blot analysis, 24% of the S. scabiei positive dogs were positive to ASA1. In contrast 82% of the dogs had antibodies towards MSA1. Immunohistochemistry (IHC) localisation of ASA1 and MSA1 supports the observation that these proteins are exposed to the host. In contrast, IHC showed that delta-GST is more confined to the mites.

Authors/Creators:Ljunggren, Erland L.
Title:Molecular analysis of Sarcoptes scabiei
Year of publishing :April 2005
Volume:2005:47
Number of Pages:63
Papers/manuscripts:
NumberReferences
ALLI. Mattsson, J.G., Ljunggren, E.L. & Bergström, K. 2001. Paramyosin from the parasitic mite Sarcoptes scabiei: cDNA cloning and heterologous expression. Parasitology 122, 555-562. II. Ljunggren, E.L., Nilsson, D. & Mattsson, J.G. 2003 Expressed sequence tag analysis of Sarcoptes scabiei. Parasitology 127, 139-145. III. Pettersson, E. U., Ljunggren, E.L. & Mattsson, J.G. 2005. Functional analysis and localisation of a delta-class glutathione-S-transferase from Sarcoptes scabiei. International Journal for Parasitology 35, 39–48 IV. Ljunggren, E.L., Bergström, K., Morrison, D.A. & Mattsson, J.G. 2005. Characterisation of an atypical antigen from Sarcoptes scabiei containing an MADF domain. Submitted manuscript.
Place of Publication:Uppsala
ISBN for printed version:91-576-7046-3
ISSN:1652-6880
Language:English
Publication Type:Doctoral thesis
Full Text Status:Public
Agris subject categories.:L Animal production > L10 Animal genetics and breeding
L Animal production > L72 Pests of animals
Subjects:Not in use, please see Agris categories
Agrovoc terms:acarina, sarcoptes scabiei, mange, gene expression, parasitoses, parasitology
Keywords:Acari, Sarcoptes scabiei, Mange, Scabies, EST, Gene expression, Gluthathione S-transferase, Immunolocalisation, Paramyosin
URN:NBN:urn:nbn:se:slu:epsilon-641
Permanent URL:
http://urn.kb.se/resolve?urn=urn:nbn:se:slu:epsilon-641
ID Code:828
Department:(VH) > Dept. of Biomedical Sciences and Veterinary Public Health
Deposited By: Erland L. Ljunggren
Deposited On:28 Apr 2005 00:00
Metadata Last Modified:02 Dec 2014 10:07

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