Borrelia burgdorferi lipoproteins are secreted to the outer surface by default.
Borrelia burgdorferi lipoproteins are secreted to the outer surface by default.
复制标题
伯氏疏螺旋体脂蛋白默认分泌到外表面。
DOI：
10.1111/j.1365-2958.2006.05039.x
复制
发表时间：
2006
影响因子：
3.6
通讯作者：
Zückert,WolframR
中科院分区：
文献类型：
--
作者：
Schulze,RyanJ;Zückert,WolframR
Borreliaspirochaetes are unique among diderm bacteria in their abundance of surface‐displayed lipoproteins, some of which play important roles in the pathogenesis of Lyme disease and relapsing fever. To identify the lipoprotein‐sorting signals inBorrelia burgdorferi, we generated chimeras between the outer surface lipoprotein OspA, the periplasmic oligopeptide‐binding lipoprotein OppAIV and mRFP1, a monomeric red fluorescent reporter protein. Localization of OspA and OppAIV point mutants showed thatBorrelialipoproteins do not follow the ‘+2’ sorting rule which targets lipoproteins to the cytoplasmic or outer membrane of Gram‐negative bacteria via the Lol pathway. Fusions of mRFP1 to short N‐terminal lipopeptides of OspA, and surprisingly OppAIV, were targeted to the spirochaetal surface. Mutagenesis of the OspA N‐terminus defined less than five N‐terminal amino acids as the minimal secretion‐facilitating signal. With the exception of negative charges, which can act as partial subsurface retention signals in certain peptide contexts, lipoprotein secretion occurs independent of N‐terminal sequence. Together, these data indicate thatBorrelialipoproteins are targeted to the bacterial surface by default, but can be retained in the periplasm by sequence‐specific signals.
