Destabilization of phospholipid model membranes by YplA, a phospholipase A2 secreted by Yersinia enterocolitica
Destabilization of phospholipid model membranes by YplA, a phospholipase A2 secreted by Yersinia enterocolitica
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DOI：
10.1016/j.chemphyslip.2004.04.009
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发表时间：
2004-09-01
影响因子：
3.4
通讯作者：
Serfis, AB
中科院分区：
文献类型：
--
作者：
Berring, E;Brancato, S;Serfis, AB
小肠结肠炎耶尔森氏菌产生毒力相关磷脂酶A（2）（YplA），其通过其鞭毛III型分泌器分泌。当YplA的N-末端59个氨基酸被去除时（得到YplA（S）），它保留磷脂酶活性;然而，它在使用胶束形式的荧光磷脂底物的水解的表观动力学方面被改变。为了更仔细地探索YplA的物理性质，使用Langmuir磷脂单层来研究YplA与生物膜的缔合。YplA和YplA（S）均与朗缪尔单层缔合，但YplA（S）似乎在低初始脂质密度下更好地相互作用，而YplA在较高密度下更好地相互作用。这可能表明YplA的N-末端在介导其与致密细胞膜的初始相互作用中起作用，这与荧光素标记的YplA可能比YplA（S）更容易与脂质体的非极性区域相互作用的光谱观察结果一致。(C)2004爱思唯尔爱尔兰有限公司保留所有权利。
Yersinia enterocolitica produces a virulence-associated phospholipase A(2) (YplA) that is secreted via its flagellar type-III secretion apparatus. When the N-terminal 59 amino acids of YplA are removed (giving YplA(S)), it retains phospholipase activity; however, it is altered with respect to the apparent kinetics of hydrolysis using fluorescent phospholipid substrates in micellar form. To explore the physical properties of YplA more carefully, Langmuir phospholipid monolayers were used to study the association of YplA with biological membranes. YPlA and YplA(S) both associate with Langmuir monolayers, but YplA(S) appears to interact better at low initial lipid densities while YplA interacts better at higher densities. This may indicate that the N-terminus of YplA has a role in mediating its initial interaction with compact cellular membranes, which is consistent with spectroscopic observations that fluorescein-labeled YplA may interact more readily with the nonpolar region of liposomes than does YplA(S). (C) 2004 Elsevier Ireland Ltd. All rights reserved.