Cuticular proteins: The neglected component

Willis, Judith H.

doi:10.1002/arch.940060402

Cited by 69 publications

(15 citation statements)

References 40 publications

(32 reference statements)

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“…Chitin and cuticular proteins are the major components of insect cuticle [21,22]. It is noteworthy to mention that the gene coding for chitin synthase, a critical enzyme for chitin synthesis [23-25], had peak expressions at the same stages in which the majority of cuticular protein genes were also highly expressed, indicating that the processes of cuticle formation were activated concurrently.…”

Section: Discussionmentioning

confidence: 99%

Expression profile of cuticular genes of silkworm, Bombyx mori

Liang

Zhang

et al. 2010

BMC Genomics

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BackgroundInsect cuticle plays essential roles in many physiological functions. During molting and metamorphosis tremendous changes occur in silkworm cuticle where multiple proteins exist and genes encoding them constitute about 1.5% of all Bombyx mori genes.ResultsIn an effort to determine their expression profiles, a microarray-based investigation was carried out using mRNA collected from larvae to pupae. The results showed that a total of 6676 genes involved in various functions and physiological pathways were activated. The vast majority (93%) of cuticular protein genes were expressed in selected stages with varying expression patterns. There was no correlation between expression patterns and the presence of conserved motifs. Twenty-six RR genes distributed in chromosome 22 were co-expressed at the larval and wandering stages. The 2 kb upstream regions of these genes were further analyzed and three putative elements were identified.ConclusionsData from the present study provide, for the first time, a comprehensive expression profile of genes in silkworm epidermal tissues and evidence that putative elements exist to allow massive production of mRNAs from specific cuticular protein genes.

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Section: Discussionmentioning

confidence: 99%

Expression profile of cuticular genes of silkworm, Bombyx mori

Liang

Zhang

et al. 2010

BMC Genomics

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“…Also, preliminary data from size fractionations of enzyme-digested cuticular peptides suggested that the inducer(s) is larger than 200 Da. Recent evidence from Candida albicans indicates that induction of an extracellular aspartyl protease is effected by peptides of more than eight residues even though its permeases do not efficiently transport peptides > 6-7 residues (Lerner & Goldman, 1993 (Rebers & Riddiford, 1988) and Hyalophora cercopia (Willis, 1987)] and two species of' Diptera [ Drosophila melanogaster (Snyder e t al., 1982) and Sarcophaga bullata (Henzel e t al., 1985)l. While there is some sequence homology between these proteins and the one protein sequenced from adult locust endocuticle (Talbo e t al., 1991) they differ markedly from the locust exocuticle proteins described above.…”

Section: Discussionmentioning

confidence: 99%

“…In general, the sequences of these proteins are characterized by three types of region: (i) regions enriched in glycine, leucine or tyrosine, (ii) hydrophobic regions wich repeats of an Ala-Ala-Pro-Ala/Val motif often preceded by tyrosine, and (iii) hydrophilic regions, dominated by amino acids with relatively large side chains. Only one adult locust endocuticular protein has been sequenced (Talbo et a/., 1991); it has sequence similarity with a number of proteins from soft larval cuticles from Lepidoptera (Rebers & Riddiford, 1988;Willis, 1987) and Diptera (Snyder e t al., 1982 ; Henzel e t a/., 1985) but is very different from adult locust exocuticle proteins. In particular there are no repeat motifs of Ala-Ala-Pro-Ala/Val.…”

Section: Potential Peptide Inducers From Insect Cuticlementioning

confidence: 99%

Partial characterization of specific inducers of a cuticle-degrading protease from the insect pathogenic fungus Metarhizium anisopliae

Paterson

Charnley

et al. 1994

Microbiology

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The insect pathogenic fungus Metarhizium anisopliae produces several extracellular cuticle-degrading proteases and evidence is consistent with one of these, PR1, which is a chymoelastase, being a determinant of pathogenicity. We have shown previously that P R l production is regulated by both carbon catabolite and nitrogen metabolite repression and also by specific induction under derepressed conditions by insect cuticle. In the present work we have established that an enzymically released proteinaceous component(s) of insect cuticle is capable of inducing PR1 (based on appearance of extracellular activity). Cuticle of the desert locust Schistocerca gregaria treated with KOH to remove protein failed to induce PR1 production, whereas cuticle treated with either chloroform or ether to remove lipids still induced PR1. Cuticle digested with either PR1 or the trypsin-like PR2 of M. anisopliae released peptides mainly in the range 150-2000 Da; addition of these peptides generated by PR1 or PR2 a t 3 pg alanine equivalents ml-1 induced PR1 production to a level similar (75 O/ O) to that obtained with untreated insect cuticle. Several amino acids and peptides which are abundant in insect cuticular protein (Ala, Gly, Ala-Ala, Ala-Ala-Ala, Ala-Pro and Pro-Ala) were tested at a range of concentrations and in restricted cultures for their ability to induce PR1. None induced the protease to the levels seen with cuticle or peptides enzymically released from cuticle, although some dimers and notably the monomers Ala and Gly gave 2-2.7-fold enhanced PR1 activity above derepressed basal levels (up to -57% of that achieved with induced synthesis on cuticle). There was evidence for more efficient uptake and/or catabolism by M. anisopliae of alanine di-and tripeptides than of monomer amino acids.

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“…Infection by these fungi is facilitated by the secretion of extracellular proteases (Charnley and St. Leger 1991; Bidochka and Khachatourians 1990; Bidochka et al 1993; St. Leger et al 1988; Willis 1987). Proteolytic enzymes appear early, in large quantities, during infection, assisting in initial host penetration and in later processes (El-Sayed et al 1993b).…”

Section: Introductionmentioning

confidence: 97%

Chitinolytic activity of the acaropathogenic fungiHirsutella thompsoniiandHirsutella necatrix

Chernin¹,

Gafni²,

Mozes-Koch³

et al. 1997

Can. J. Microbiol.

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Two isolates of the acaropathogenic fungus Hirsutella thornpsonii (Nos. 255 and 414), and Hirsutella necatrix, were able to produce and excrete chitinolytic enzymes. A chitobiase of >205 kDa was excreted by all fungi and a chitobiase of 112 kDa only by isolate 414. An endochitinase of 162 kDa was excreted by isolate 414 and two endochitinases of 66 and 38 kDa were excreted by isolate 255. Both H. thompsonii isolates produced chitinolytic enzymes only under inducible conditions, in the presence of colloidal chitin as the sole source of carbon. Hirsutella necatrix produced a chitobiase constitutively when grown in the presence of glucose. In addition to chitinolytic enzymes, the H. thompsonii isolates excreted proteolytic activities, including elastase, as well as a-esterase and a-amylase activities. Hirsutella necatrix was unable to use casein, milk powder, or elastin as the sole carbon source. The acaropathogenicity of these isolates was assayed on the carmine spider mite (Tetranychus cinnabarinus). Isolates 414 and 255 and H. necatrix killed ca. 80, 35, and 15%, respectively, of the infected mites. The role of chitinolytic and other enzymatic activities in the acaropathogenicity of these fungi is discussed.RCsume : Les auteurs ont Ctabli que deux isolats du champignon acaropathogkne Hirsutella thompsonii (no 255 et 414), ainsi que le Hirsutella necatrix, sont capables de produire et d'excreter des enzymes chitinolytiques. Ces champignons ont tous excrttk une chitobiase de >250 kDa, tandis que seul I'isolat 414 a excrCtC une chitobiase de 112 kDa. L'isolat 414 a excrCtC une endochitinase de 162 kDa, alors que I'isolat 255 en a excrttC deux de 66 et 38 kDa. Les deux isolats de H. thompsonii ont produit des enzymes chitinolytiques, mais seulement dans des conditions d'induction en prCsence de chitine colloidale comme seule source de carbone. Le H. necatrix, cultivC en prCsence de glucose, a produit une chitobiase de faqon constitutive. En plus des enzymes chitinolytiques, les isolats de H. thompsonii ont excrCtC des enzymes proteolytiques dont I'Clastase, I'a-estCrase et I'a-amylase. Le H. necatrix n'a pu utiliser la casCine, la poudre de lait ou 1'Clastine comme seule source de carbone. Le potentiel acaropathogkne de ces isolats a Ct C test6 sur des tCtranyques carminks (Tetranychus cinnabarinus). Les isolats 414 et 255 et le H. necatrix ont tuC respectivement environ 80, 35 et 15% des tktranyques infect&. Le r61e des enzymes chitinolytiques et des autres enzymes dans le caractkre acaropathogkne de ces champignons est discutC.

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Cuticular proteins: The neglected component

Cited by 69 publications

References 40 publications

Expression profile of cuticular genes of silkworm, Bombyx mori

Expression profile of cuticular genes of silkworm, Bombyx mori

Partial characterization of specific inducers of a cuticle-degrading protease from the insect pathogenic fungus Metarhizium anisopliae

Chitinolytic activity of the acaropathogenic fungiHirsutella thompsoniiandHirsutella necatrix

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