MODE OF ACTION OF PEDIOCIN ACH FROM PEDIOCOCCUS-ACIDILACTICI-H ON SENSITIVE BACTERIAL STRAINS

MODE OF ACTION OF PEDIOCIN ACH FROM PEDIOCOCCUS-ACIDILACTICI-H ON SENSITIVE BACTERIAL STRAINS
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DOI:
10.1111/j.1365-2672.1991.tb03782.x
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发表时间:
1991-01-01
期刊:
JOURNAL OF APPLIED BACTERIOLOGY
影响因子:
--
通讯作者:
KALCHAYANAND, N
KALCHAYANAND, N
中科院分区:
其他
文献类型:
--
作者:
BHUNIA, AK;JOHNSON, MC;KALCHAYANAND, N

文献摘要

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从酸链球菌H中分离出的多肽--儿茶素ACh能与植物乳杆菌NCDO 955及其耐药突变株NCDO 955细胞表面结合,但不能与革兰氏阴性菌结合。敏感细胞在用佩去菌素ACh处理后,失去了细胞内的K+离子,这是一种吸收紫外线的物质,变得对ONPG更具渗透性,在某些菌株中,还被溶解。在pH为6.0时,儿茶素与ACh的结合量最大。几种盐的阴离子抑制了儿茶素ACh的结合,但这一点被增加浓度的Pediocin ACh所克服。用1%十二烷基硫酸钠、4mol/L盐酸胍、几种有机溶剂和几种酶处理敏感细胞,并不能减少随后与儿茶素的结合。部分纯化的敏感菌株的细胞壁也能与哌替卡菌素结合。然而,处理细胞壁以去除脂磷壁酸阻止了结合。因此,这些分子可能是儿茶素ACh的结合部位之一。
The peptide, pediocin AcH, from Pediococcus acidilactici H binds to the cell surface of Lactobacillus plantarum NCDO 955, its resistant mutant and several other sensitive and resistant Gram-positive bacteria but not to Gram-negative bacteria. Sensitive cells, following treatment with pediocin AcH, lost intracellular K+ ions, u.v.-absorbing materials, became more permeable to ONPG and, in some strains, lysed. Binding of pediocin AcH was maximum at pH 6.0. Anions of several salts inhibited binding of pediocin AcH but this was overcome by increased concentrations of pediocin AcH. Treatment of sensitive cells with 1 % SDS, 4 mol/l guanidine-HCl, several organic solvents and enzymes did not reduce subsequent binding of pediocin AcH. Partially purified cell wall from a sensitive strain was also able to bind pediocin AcH. However, treatment of the cell walls to remove lipoteichoic acid prevented binding. These molecules might, therefore, be one of the binding sites of pediocin AcH.