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DOI: | 10.11686/cyxb20100621 |
Web URL(s): | http://cyxb.lzu.edu.cn/EN/article/downloadArticleFile.do?attachType=PDF&id=2843 Last checked: 02/11/2016 Requires: PDF Reader |
Publication Type:
| Report |
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. |
Publishing Information: | [Lanzhou Shi, China]: ["Cao Ye Xue Bao" Bian Ji Wei Yuan Hui] |
# of Pages: | 7 |
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." |
Language: | Chinese |
References: | 28 |
Note: | Abstract also appears in English "Sum No. 89" Figures Tables |
| 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 |
| Web URL(s): http://cyxb.lzu.edu.cn/EN/article/downloadArticleFile.do?attachType=PDF&id=2843 Last checked: 02/11/2016 Requires: PDF Reader |
| MSU catalog number: b10289426 |
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