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负责蜜蜂抗菌肽抗菌作用的氨基酸残基的功能图谱分析。

Functional mapping of amino acid residues responsible for the antibacterial action of apidaecin.

作者信息

Taguchi S, Ozaki A, Nakagawa K, Momose H

机构信息

Department of Biological Science and Technology, Science University of Tokyo, Chiba, Japan.

出版信息

Appl Environ Microbiol. 1996 Dec;62(12):4652-5. doi: 10.1128/aem.62.12.4652-4655.1996.

DOI:10.1128/aem.62.12.4652-4655.1996
PMID:8953737
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC168292/
Abstract

Functional mapping was carried out to address the amino acid residues responsible for the activity of the antibacterial peptide apidaecin from the honeybee by an in vivo assay system developed previously. The C-terminal region and many of the proline and arginine residues which are present at high frequency in apidaecin were found to play an important role in its antibacterial activity.

摘要

通过先前开发的体内测定系统进行功能图谱分析，以确定负责蜜蜂抗菌肽apidaecin活性的氨基酸残基。发现apidaecin中高频出现的C末端区域以及许多脯氨酸和精氨酸残基在其抗菌活性中起重要作用。

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本文引用的文献

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Apidaecin multipeptide precursor structure: a putative mechanism for amplification of the insect antibacterial response.蜜蜂防御肽多肽前体结构：昆虫抗菌反应放大的一种推测机制。
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Apidaecin-type peptide antibiotics function through a non-poreforming mechanism involving stereospecificity.
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In vivo monitoring system for structure-function relationship analysis of the antibacterial peptide apidaecin.
Appl Environ Microbiol. 1994 Oct;60(10):3566-72. doi: 10.1128/aem.60.10.3566-3572.1994.
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Biodiversity of apidaecin-type peptide antibiotics. Prospects of manipulating the antibacterial spectrum and combating acquired resistance.
J Biol Chem. 1994 Oct 21;269(42):26107-15.
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