Annotation and analysis of a large cuticular protein family with the R&amp;R Consensus in Anopheles gambiae

Cornman, Robert S.; Togawa, Toru; Dunn, William A.; He, Ningjia; Emmons, Aaron C.; Willis, Judith H.

doi:10.1186/1471-2164-9-22

Cited by 109 publications

(128 citation statements)

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“…The number of chitin-binding cuticular proteins in different insect genomes varies significantly (Magkrioti et al 2004;Weinstock et al 2006;Karouzou et al 2007;Cornman et al 2008;Futahashi et al 2008;Richards et al 2008;Willis 2010;Gilbert 2011, Chap. 5).…”

Section: Resultsmentioning

confidence: 99%

“…5) and form a proteinaceous matrix in which chitin fibers are embedded (Neville 1975;Papandreou et al 2010). CP-chitin interactions are necessary for the normal structure and physical properties of cuticle (Andersen et al 1995;Rebers and Willis 2001;Karouzou et al 2007;Cornman et al 2008;Moussian 2010). Over half of the known cuticular proteins contain chitin-binding domains, including the Rebers & Riddiford (R&R) motif (two major groups, RR-1 and RR-2, and a minor form, RR-3), Tweedle motif, and chtDB2 domain (Rebers and Riddiford 1988;Magkrioti et al 2004;Cornman et al 2008;Jasrapuria et al 2010;Willis 2010;Andersen 2011;Gilbert 2011, Chap.…”

mentioning

confidence: 99%

“…Cuticular proteins (CPs), the principal structural constituents of cuticle, are encoded by more than 100 genes in known insect genomes (Andersen et al 1995;Willis et al 2005;Weinstock et al 2006;Karouzou et al 2007;Cornman et al 2008;Futahashi et al 2008;Richards et al 2008;Cornman and Willis 2009;Gilbert 2011, Chap. 5) and form a proteinaceous matrix in which chitin fibers are embedded (Neville 1975;Papandreou et al 2010).…”

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Mutation of a Cuticular Protein,BmorCPR2, Alters Larval Body Shape and Adaptability in Silkworm,Bombyx mori

et al. 2014

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Cuticular proteins (CPs) are crucial components of the insect cuticle. Although numerous genes encoding cuticular proteins have been identified in known insect genomes to date, their functions in maintaining insect body shape and adaptability remain largely unknown. In the current study, positional cloning led to the identification of a gene encoding an RR1-type cuticular protein, BmorCPR2, highly expressed in larval chitin-rich tissues and at the mulberry leaf-eating stages, which is responsible for the silkworm stony mutant. In the Dazao-stony strain, the BmorCPR2 allele is a deletion mutation with significantly lower expression, compared to the wild-type Dazao strain. Dysfunctional BmorCPR2 in the stony mutant lost chitin binding ability, leading to reduced chitin content in larval cuticle, limitation of cuticle extension, abatement of cuticle tensile properties, and aberrant ratio between internodes and intersegmental folds. These variations induce a significant decrease in cuticle capacity to hold the growing internal organs in the larval development process, resulting in whole-body stiffness, tightness, and hardness, bulging intersegmental folds, and serious defects in larval adaptability. To our knowledge, this is the first study to report the corresponding phenotype of stony in insects caused by mutation of RR1-type cuticular protein. Our findings collectively shed light on the specific role of cuticular proteins in maintaining normal larval body shape and will aid in the development of pest control strategies for the management of Lepidoptera.T HE cuticle covering the entire body surface of insects not only participates in defense against pathogens and adverse environmental factors, but is also indispensable for constructing and maintaining external morphological characteristics and locomotion during the entire developmental process (Wigglesworth 1957;Delon and Payre 2004;Moussian et al. 2005). Therefore, the cuticle greatly enhances survival ability and adaptability of insects, ensuring its continued existence as one of the most successful life forms in the animal kingdom.The cuticle is a complex composite material mainly comprising chitin fibers and proteins (Andersen et al. 1995;Moussian 2010). Chitin is the polymer of b-1,4-linked N-acetyl-D-glucosamine (Gilbert 2011, Chap. 7). In procuticles, chitin fibers are arranged in laminae in an antiparallel manner and superimpose each other, forming sheets of fibrils that are stacked in a helicoidal fashion, maintaining cuticle structure, elasticity, and stability (Bouligand 1965;Neville and Luke 1969;Moussian 2010). In terrestrial insects, the chitin content is positively correlated with body size, suggesting a close relationship with cuticle extension and expansion (Merzendorfer and Zimoch 2003;Lease and Wolf 2010).Cuticular proteins (CPs), the principal structural constituents of cuticle, are encoded by more than 100 genes in known insect genomes (Andersen et al. 1995 The soft, flexible cuticle of Lepidoptera larvae not only bears pressure from ...

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Section: Resultsmentioning

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Mutation of a Cuticular Protein,BmorCPR2, Alters Larval Body Shape and Adaptability in Silkworm,Bombyx mori

et al. 2014

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“…Indeed, more than 200 putative CP genes have been identified in the malaria mosquito, Anopheles gambiae (Cornman et al, 2008) and the silkworm, Bombyx mori (Futahashi et al, 2008). T. castaneum has 108 genes encoding CP-like proteins (Dittmer et al, 2012;Richards et al, 2008).…”

Section: Introductionmentioning

confidence: 99%

Two major cuticular proteins are required for assembly of horizontal laminae and vertical pore canals in rigid cuticle of Tribolium castaneum

Noh

Kramer

Muthukrishnan

et al. 2014

Insect Biochemistry and Molecular Biology

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“…For the manual CP annotations we have done in Anopheles (6,8,31,42), Drosophila melanogaster (27), Apis (18), Nasonia (48), Glossina (22), and Strigamia (5), all we had to do was go to a website prepared by the original sequencing team. Another factor in facilitating annotation and providing insights in function has www.annualreviews.org • Arthropod Proteomics and Genomicsbeen the implementation of comprehensive websites such as FlyBase (http://flybase.org/) and VectorBase (https://www.vectorbase.org/).…”

Section: Still Lookingmentioning

confidence: 99%

The Evolution and Metamorphosis of Arthropod Proteomics and Genomics

Willis

2018

Annu. Rev. Entomol.

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This article presents an overview of the development of techniques for analyzing cuticular proteins (CPs), their transcripts, and their genes over the past 50 years based primarily on experience in the laboratory of J.H. Willis. It emphasizes changes in the kind of data that can be gathered and how such data provided insights into the molecular underpinnings of insect metamorphosis and cuticle structure. It describes the techniques that allowed visualization of the location of CPs at both the anatomical and intracuticular levels and measurement of the appearance and deployment of transcripts from CP genes as well as what was learned from genomic and transcriptomic data. Most of the early work was done with the cecropia silkmoth, Hyalophora cecropia, and later work was with Anopheles gambiae.

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Annotation and analysis of a large cuticular protein family with the R&R Consensus in Anopheles gambiae

Cited by 109 publications

References 46 publications

Mutation of a Cuticular Protein,BmorCPR2, Alters Larval Body Shape and Adaptability in Silkworm,Bombyx mori

Mutation of a Cuticular Protein,BmorCPR2, Alters Larval Body Shape and Adaptability in Silkworm,Bombyx mori

Two major cuticular proteins are required for assembly of horizontal laminae and vertical pore canals in rigid cuticle of Tribolium castaneum

The Evolution and Metamorphosis of Arthropod Proteomics and Genomics

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