Literature DB >> 27744002

Immunolocalization of cuticular proteins in Johnston's organ and the corneal lens of Anopheles gambiae.

Laura Vannini1, Judith H Willis2.   

Abstract

Previous work with EM immunolocalization examined the intracuticular placement of several antibodies directed against cuticular proteins (CPs) in various structures of Anopheles gambiae. Those structures had long stretches of fairly uniform cuticle. We have now used 19 antibodies directed against members of five CP families on two adult structures with considerable complexity, Johnston's organ and the corneal lens of the compound eye. We also localized chitin with colloidal-gold labeled wheat germ agglutinin. Twelve of these antibodies recognized structures in Johnston's organ. Only 6 were detected in the outer pedicel wall, but the internal structures were more complex with distinct distributions of members of the five CP families in six different structures. The corneal lens had four distinct regions of laminar cuticle. Thirteen of the 15 members of the CPR family were detected, none from the other CP families. Specific antibodies were localized to different regions and in different laminae within a region. The specificity of deployment of cuticular proteins revealed in this study is helping to explain why An. gambiae allocates about 2% of its protein coding genes to structural CPs.
Copyright © 2016 Elsevier Ltd. All rights reserved.

Entities:  

Keywords:  Antennae; Compound eye; Cuticular laminae; EM immunolocalization; Mosquito

Mesh:

Substances:

Year:  2016        PMID: 27744002      PMCID: PMC5228451          DOI: 10.1016/j.asd.2016.10.006

Source DB:  PubMed          Journal:  Arthropod Struct Dev        ISSN: 1467-8039            Impact factor:   2.010


  24 in total

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Authors:  Laura Vannini; Judith H Willis
Journal:  Arthropod Struct Dev       Date:  2016-10-30       Impact factor: 2.010

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5.  Contributions of cuticle permeability and enzyme detoxification to pyrethroid resistance in the major malaria vector Anopheles gambiae.

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