中华绒螯蟹微孢子虫全基因组分泌蛋白的预测分析

doi:10.16378/j.cnki.1003-1111.20202

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Abstract In this study, we predict the secretory proteins of microsporidium Hepatospora eriocheir genome parasited in Chinese mitten crab Eriocheir sinensis with the EuSecPred 2.0 and annotate for secreted protein function, characteristics and the sequence analysis. The length of secreted proteins was found to be primarily changed from 30 amino acids to 300 amino acids, with length of signal peptide from 11 amino acids to 23 amino acids. The signal peptide cleavage site was mainly composed of hydrophobic amino acids. Many key proteins were found by functional annotation of the secretory proteins such as haemaglutinin-esterase, methyltransferase EZH1, and serine/threonine protein kinase. Motif analysis revealed that there was a S[NS]N[TI][FI]VI[IGD][RG]VRC motif in signal peptides which predicted secreted proteins were involved in the physiological activities of H. eriocheir, host cell cycle regulation and immune response. The findings provide important basis for screening disease-related candidate factors and exploring the infection mechanism.

Key words： Hepatospora eriocheir secretory protein genome signal peptide motif

Received: 08 September 2020

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	Articles by authors
	NING Zijian
	KOU Shiyu
	BAO Jie
	JIANG Hongbo

Cite this article:

NING Zijian,KOU Shiyu,BAO Jie, et al. Genome-Wide Prediction and Analysis of Secretory Proteins of Microsporidium Hepatospora eriocheir Parasited in Chinese Mitten Crab Eriocheir sinensis[J]. Fisheries Science, 2022, 41(2): 280-288.

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https://www.shchkx.com/EN/10.16378/j.cnki.1003-1111.20202 OR https://www.shchkx.com/EN/Y2022/V41/I2/280

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