Evidence map›Paper›PMID 27717796›Full record

ArticleArthropod structure & development2017

Localization of RR-1 and RR-2 cuticular proteins within the cuticle of Anopheles gambiae.

Laura Vannini, Judith H Willis

Abstract read
In one paragraph

Article in Arthropod structure & development, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 papers.

0numbers the graph read from it
0cells of the map it votes in
31citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

What it found

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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

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Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

31 citing papers in PubMed.

  1. Multimodal Insecticidal Activity ofInternational journal of molecular sciences · 2026
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  7. A Leg Cuticle Protein Enhances the Resistance ofInternational journal of molecular sciences · 2025
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4 · The record

Corrections and comments

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5 · Who and what money

Authors and funding

2 authors.

Laura VanniniDepartment of Cellular Biology, University of Georgia, Athens, GA 30602, USA.
Judith H WillisDepartment of Cellular Biology, University of Georgia, Athens, GA 30602, USA. Electronic address: jhwillis@uga.edu.

Funding

Cuticular proteins of Anopheles gambiaeR01AI055624 · NIAID · UNIVERSITY OF GEORGIA (UGA) · PI WILLIS, JUDITH · 2004 to 2014
$2.8M
NIAID NIH HHS R01 AI055624
6 · The paper itself

Abstract

The largest arthropod cuticular protein family, CPR, has the Rebers and Riddiford (R&R) Consensus that in an extended form confers chitin-binding properties. Two forms of the Consensus, RR-1 and RR-2, have been recognized and initial data suggested that the RR-1 and RR-2 proteins were present in different regions within the cuticle itself. Thus, RR-2 proteins would contribute to exocuticle that becomes sclerotized, while RR-1s would be found in endocuticle that remains soft. An alternative, and more common, suggestion is that RR-1 proteins are used for soft, flexible cuticles such as intersegmental membranes, while RR-2s are associated with hard cuticle such as sclerites and head capsules. We used TEM immunogold detection to localize the position of several RR-1 and RR-2 proteins in the cuticle of Anopheles gambiae. RR-1s were localized in the procuticle of the soft intersegmental membrane except for one protein found in the endocuticle of hard cuticle. RR-2s were consistently found in hard cuticle and not in flexible cuticle. All RR-2 antibodies localized to the exocuticle and four out of six were also found in the endocuticle. Hence the location of RR-1s and RR-2s depends more on properties of individual proteins than on either hypothesis.

Indexed as

Gene Expression RegulationAnimalsAnophelesAntibodiesCell MembraneChitinGene Expression Regulation, DevelopmentalImmunohistochemistryInsect ProteinsMicroscopy, ElectronMicroscopy, Electron, TransmissionPeptidesProtein BindingAntibodiesChitincuticle proteins, insectsInsect ProteinsPeptidesEM immunolocalizationEndocuticleExocuticleIntersegmental membraneRebers & Riddiford ConsensusSclerite

Identifiers

PMID27717796
PMCPMC5292290

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Registered trials

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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.