Identification of two new peritrophic membrane proteins from larval Trichoplusia ni: structural characteristics and their functions in the protease rich insect gut

Wang, Ping; Li, Guoxun; Granados, Robert R.

doi:10.1016/j.ibmb.2003.10.001

Cited by 85 publications

(104 citation statements)

References 30 publications

Supporting

Mentioning

Contrasting

Unclassified

Order By: Relevance

“…SDS-PAGE showed that its molecular weight was 116 kDa, which was higher than predicted. This is similar with most other PM proteins, including TnCBP, whose predicted molecular weight is 120 kDa but SDS-PAGE shows its actual weight to be almost 200 kDa (Wang et al, 2004). This phenomenon might be associated with protein modification mechanisms in eukaryotic cells, such as glycosylation, given that SeCBP66 was predicted to have five potential N-glycosylation sites located at the gap between CBD2 and CBD7.…”

Section: Discussionsupporting

confidence: 70%

“…To date, several PM proteins have been identified from various insect species, including the larvae of Lepidoptera, Diptera, and Coleoptera, and other agriculturally important insects (Wang et al, 2004;Guo et al, 2005;Zhang and Guo, 2011;Liu et al, 2014;Zhao et al, 2014). One class of the major PM proteins includes members with multiple chitin-binding domains (CBDs) that can only be removed by mild or strong denaturants, which cross-link with chitin fibrils to form the PM Granados, 1997, 2001).…”

Section: Introductionmentioning

confidence: 99%

See 1 more Smart Citation

Structural and biochemical characteristics of chitin-binding protein SeCBP66 from Spodoptera exigua (Hübner)

et al. 2016

View full text Add to dashboard Cite

ABSTRACT. Peritrophic membrane proteins are important components of the insect peritrophic membrane. A novel cDNA gene encoding a chitin-binding protein, named secbp66, was identified by immunization screening of the cDNA library of Spodoptera exigua. The full length of secbp66 is 1806 bp, which encodes 602 amino acids. The predicted weight of the protein is 64.2 kDa. Bioinformatic analysis showed that a signal peptide composed of 17 amino acids located at the N-terminal of SeCBP66 contained seven tandem putative Type-II functional chitin-binding domains and five potential N-glycosylation sites, but no O-linked glycosylation sites. To study the properties of SeCBP66, recombinant SeCBP66 was successfully expressed in the insect cell line BTI-Tn-5B1-4 with a Bac-to-Bac expression system. A chitin binding experiment showed that the recombinant SeCBP66 protein could bind to chitin strongly. This study of the novel chitin-

show abstract

Section: Discussionsupporting

confidence: 70%

Section: Introductionmentioning

confidence: 99%

Structural and biochemical characteristics of chitin-binding protein SeCBP66 from Spodoptera exigua (Hübner)

et al. 2016

View full text Add to dashboard Cite

show abstract

“…All peritrophins contain cysteine-rich regions, which form chitin-binding domains and bind to chitin (Tellam et al, 1999;Wang et al, 2004). Peritrophins with chitin-binding domains containing 6, 8, and 10 cysteine residues are classified as types A, B, and C, respectively (Tellam et al, 1999).…”

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

View full text Add to dashboard Cite

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.

show abstract

“…Class 3 proteins from several Lepidoptera and Diptera often contain one or more chitin-binding 'peritrophin A' domains of 60-75 amino acid residues with a conserved pattern of cysteine and aromatic residues (InterPro IPR002557). Most contain multiple chitin-binding domains which may provide cross-linking between chitin fibrils even when partially degraded by digestive proteinases (Wang et al, 2004;Shao et al, 2005). A subset of these proteins is insect intestinal mucins (IIM) which are large with highly O-glycosylated mucin domains interspersed with peritrophin domains, hence the suggestion that the PM is an analogue of vertebrate mucus reinforced by chitin.…”

Section: Introductionmentioning

confidence: 99%

Proteomic analysis of the peritrophic matrix from the gut of the caterpillar, Helicoverpa armigera

Campbell

Cao

Hines

et al. 2008

Insect Biochemistry and Molecular Biology

103

107

View full text Add to dashboard Cite

Identification of two new peritrophic membrane proteins from larval Trichoplusia ni: structural characteristics and their functions in the protease rich insect gut

Cited by 85 publications

References 30 publications

Structural and biochemical characteristics of chitin-binding protein SeCBP66 from Spodoptera exigua (Hübner)

Structural and biochemical characteristics of chitin-binding protein SeCBP66 from Spodoptera exigua (Hübner)

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

Proteomic analysis of the peritrophic matrix from the gut of the caterpillar, Helicoverpa armigera

Contact Info

Product

Resources

About