Genes encoding proteins with peritrophin A-type chitin-binding domains in Tribolium castaneum are grouped into three distinct families based on phylogeny, expression and function

Jasrapuria, Sinu; Arakane, Yasuyuki; Osman, Gamal; Kramer, Karl J.; Beeman, Richard W.; Muthukrishnan, Subbaratnam

doi:10.1016/j.ibmb.2010.01.011

Cited by 153 publications

(185 citation statements)

References 43 publications

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“…Importantly, Obst-A homologs were identified in arthropods and nematodes (Fig. 2C) (12,30). This suggests that a similar mechanism may exist to control chitin ECM degradation among chitinous invertebrates.…”

Section: Discussionmentioning

confidence: 85%

Obstructor-A Is Required for Epithelial Extracellular Matrix Dynamics, Exoskeleton Function, and Tubulogenesis

Petkau

Wingen

Jussen

et al. 2012

Journal of Biological Chemistry

111

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Background:The extracellular matrix (ECM) is essential for protection and development of epithelial tissues. Results: Obstructor-A (Obst-A) organizes a core complex with chitin modifiers and enzymes to protect ECM from premature degradation. Conclusion: Obst-A is required for growth control, tubulogenesis, wound healing, and epithelial integrity. Significance: This novel mechanism is crucial for understanding ECM dynamics of epithelial tissues.

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Section: Discussionmentioning

confidence: 85%

Obstructor-A Is Required for Epithelial Extracellular Matrix Dynamics, Exoskeleton Function, and Tubulogenesis

Petkau

Wingen

Jussen

et al. 2012

Journal of Biological Chemistry

111

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“…An analysis of the Bt-CI peptide sequence revealed its similarity to other serine protease inhibitor family members, with features including ten conserved cysteine residues (Bania et al, 1999;Rhoads et al, 2000a, b). Bt-CBP possesses the chitin binding peritrophin-A domain, which contains typical features consistent with other chitin-binding proteins, including six conserved cysteine residues (Jasrapuria et al, 2010;Toprak et al, 2010). Additionally, Bt-CI and Bt-CBP share 96% peptide sequence identities with the homologous sequences of B. impatiens.…”

Section: Resultsmentioning

confidence: 91%

“…The peritrophin A domain, consisting of six cysteines, is the most common (Tellam et al, 1999;. Additionally, proteins with chitin-binding domains are widely distributed in various tissues of insects (Jasrapuria et al, 2010;Toprak et al, 2010).…”

Section: Introductionmentioning

confidence: 99%

Molecular Cloning and Characterization of Chymotrypsin Inhibitor and Chitin-Binding Protein Homologs from the Bumblebee Bombus terrestris

Qiu¹,

Yoon²,

Jin³

2012

International Journal of Industrial Entomology

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The bumblebee Bombus terrestris is widely used in greenhouses to pollinate crops. Here, we report the molecular cloning and characterization of chymotrypsin inhibitor and chitin-binding protein homologs from B. terrestris. Two cDNAs encoding chymotrypsin inhibitor (Bt-CI) and chitin-binding protein (Bt-CBP) homologs were cloned from B. terrestris. Gene sequence analysis showed that Bt-CI gene consists of three exons encoding 75 amino acids, including a predicted 20-amino acid signal peptide, while Bt-CBP consists of two exons encoding 78 amino acids, including a predicted 26-amino acid signal peptide. The mature Bt-CI and Bt-CBP peptides contain ten and six conserved cysteine residues, respectively. Database searches using the deduced sequences of Bt-CI and Bt-CBP showed similarity to those from B. impatiens (96% peptide sequence identities). Bt-CI and Bt-CBP were expressed in both the venom gland and fat body of B. terrestris worker bees. The recombinant Bt-CI and Bt-CBP peptides were expressed in baculovirusinfected insect cells. Taken together, our findings describe the molecular characterization of Bt-CI and Bt-CBP from B. terrestris.

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“…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. 5).…”

mentioning

confidence: 99%

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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Genes encoding proteins with peritrophin A-type chitin-binding domains in Tribolium castaneum are grouped into three distinct families based on phylogeny, expression and function

Cited by 153 publications

References 43 publications

Obstructor-A Is Required for Epithelial Extracellular Matrix Dynamics, Exoskeleton Function, and Tubulogenesis

Obstructor-A Is Required for Epithelial Extracellular Matrix Dynamics, Exoskeleton Function, and Tubulogenesis

Molecular Cloning and Characterization of Chymotrypsin Inhibitor and Chitin-Binding Protein Homologs from the Bumblebee Bombus terrestris

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

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