Full TGIF Record # 237665
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Web URL(s):http://cyxb.lzu.edu.cn/EN/article/downloadArticleFile.do?attachType=PDF&id=2843
    Last checked: 02/11/2016
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Author(s):Zhou, Hong-xu; Li, Chang-you; Li, Guo-xun
Author Affiliation:A Center for Advanced Invertebrate Cell Culture and Cell Engineering, Qingdao Agricultural University, Qingdao, China
Title:Molecular cloning and sequencing of cDNAs of the novel protein Ho-Peritrophin3 fromthe peritrophic matrix of Holotrichia oblita, a turfgrass pest
Source:[Caoye Xuebao] [Acta Prataculturae Sinica]. Vol. 19, No. 6, December 20 2010, p. 147-153.
# of Pages:7
Publishing Information:[Lanzhou Shi, China]: ["Cao Ye Xue Bao" Bian Ji Wei Yuan Hui]
Abstract/Contents:"Holotrichia oblita is an important turfgrass pest, whose peritrophic matrix is a potential target for biocontrol of pest insects. The peritrophic matrix proteins of H. oblita were studied by screening with a PM protein polyclonal antiserum from Helicoverpa armigera. One positive cDNA clone name Ho-Peritrophin3, with a size of 1737 bp and a polyadenylation signal of AATAAA upstream of the polyA tail, was screened and sequenced from the library. The longest open reading frame of Ho-Peritrophin3 coded for 528 amino acids, which were mostly similar to Ho-Preitrophin2 of H. oblita, with a similarity of 64.9%. Ho-Peritrophin3, with a little O-linked glycosylation sites, contained five chitin binding domains, all of which consisted of six conserved cysteine residues, while Ho-Peritrophin1 and Ho-Peritrophin2 found in the PM of H. oblita contained only four cysteine residues at the C-terminal. No mucin-like domain was found in the Ho-Peritrophin3 sequence. The cleavage sites of trypsin and chymotrypsin mainly lay inside of CBDs in the Ho-Peritrophin3, and were protected by the intradomain disulfide bonds, so they can resist enzymes and exert of physiological function in the midgut. Compared with Ho-Peritrophin1 and Ho-Peritrophin2, 36.3% of 107 amino acids downstream of the fifth CBD belonged to the cleavage sites of trypsin and chymotrypsin. Further study is necessary to explain why Ho-Peritrophin3 can exist in the midgut in the presence of abundant proteinase."
Note:Abstract also appears in English
"Sum No. 89"
ASA/CSSA/SSSA Citation (Crop Science-Like - may be incomplete):
Zhou, H.-x., C.-y. Li, and G.-x. Li. 2010. Molecular cloning and sequencing of cDNAs of the novel protein Ho-Peritrophin3 fromthe peritrophic matrix of Holotrichia oblita, a turfgrass pest. (In Chinese) [Caoye Xuebao] [Acta Prataculturae Sinica]. 19(6):p. 147-153.
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DOI: 10.11686/cyxb20100621
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    Last checked: 02/11/2016
    Requires: PDF Reader
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MSU catalog number: b10289426
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