Borrelia burgdorferi surface-located Lmp1 protein processed into region-specific polypeptides that are critical for microbial persistence.
Borrelia burgdorferi surface-located Lmp1 protein processed into region-specific polypeptides that are critical for microbial persistence.
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DOI:
10.1111/cmi.12855
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发表时间:
2018-09
影响因子:
3.4
通讯作者:
Pal U
中科院分区:
文献类型:
--
作者:
Zhuang X;Yang X;Altieri AS;Nelson DC;Pal U
One of the Borrelia burgdorferi virulence determinants, annotated as Lmp1, is a surface-exposed, conserved and potential multi-domain protein involved in various functions in spirochete infectivity. Lmp1 contributes to host-pathogen interactions and evasion of host adaptive immunity by spirochetes. Here we show that in diverse B. burgdorferi species, Lmp1 exists as distinct, region-specific and lower molecular mass polypeptides encompassing one or more domains, including independent N-terminal and middle regions and a combined middle and C-terminal region. These polypeptides originate from complex posttranslational maturation events, partly supported by a periplasmic serine protease termed as BbHtrA. While spirochete persistence in mice is independently supported by domain-specific Lmp1 polypeptides, transmission of B. burgdorferi from ticks to mammals requires essential contributions from both N-terminal and middle regions. Interference with the functions of Lmp1 domains or their complex posttranslational maturation events may aid in development of novel therapeutic strategies to combat infection and transmission of pathogens.
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影响因子:
3.6
作者:
Kariu T;Yang X;Marks CB;Zhang X;Pal U
通讯作者:
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影响因子:
3.7
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3.2
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Schutzer, Steve E.
影响因子:
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