梅毒螺旋体外膜蛋白功能及应用的研究进展
摘要
球严重的公共卫生问题。梅毒螺旋体外膜缺乏内毒素，也不产生明显的毒力因子，其外膜蛋白在维持病原性和调节宿主免
疫反应中起着关键作用，有潜在的免疫诊断价值和较强疫苗研究作用。本文对已发现的重要梅毒螺旋体外膜蛋白的结构、
生物学功能，特别是致病机制和潜在诊断价值方面的研究进行了概述，为梅毒防治以及公共卫生领域取得更显著的突破提
供新的思路。
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[1]Rosanna W Peeling, David Mabey, Mary L Kamb, et al.
Syphilis[J]. Nat Rev Dis Primers. 2017,3:17073.
[2]Jinlin Chen, Jielite Huang, Zhuoran Liu,et al. Treponema
pallidum outer membrane proteins: current status and
prospects[J]. Pathog Dis. 2022, 80(1):ftac023.
[3]Justin D Radolf, Sanjiv Kumar. The Treponema pallidum
Outer Membrane[J]. Curr Top Microbiol Immunol. 2018,415:1-38.
[4]Xi Luo, Xiaohong Zhang, Lin Gan, et al. The outer
membrane protein Tp92 of Treponema pallidum induces human
mononuclear cell death and IL-8 secretion[J]. 2018,22(12):6039-
6054.
[5]Xie Y, Xu M, Wang C, et al. Diagnostic value of
recombinant Tp0821 protein in serodiagnosis for syphilis[J]. Lett
Appl Microbiol. 2016,62(4):336-343.
[6]Ning Wu, Ni Li, Liping Hu, et al. Immunogenicity and
immunoreactivity of Tp0821 recombinant protein from Treponema
pallidum[J]. Mol Med Rep. 2017,16(1):851-856.
[7] 阳建 , 杨荣志 , 唐诚 . 梅毒螺旋体四种不同膜蛋白在
血清学诊断中的应用研究 [J]. 临床和实验医学杂志 , 2015,
14(06): 457-460.
[8]Kamfai Chan, Thayer Nasereddin, Laura Alter, et al.
Treponema pallidum Lipoprotein TP0435 Expressed in Borrelia
burgdorferi Produces Multiple Surface/Periplasmic Isoforms and
mediates Adherence[J]. Sci Rep. 2016, 10:6:25593.
[9]Karolin Pollok, Ronja Mothes, Carolin Ulbricht, et al.The
chronically inflamed central nervous system provides niches
for long-lived plasma cells. Acta Neuropathol Commun[J].
2017,5(1):88.
[10]Shun Xiong, Zhaoping Liu, Xiaohong Zhang, et al.
Resurgence of syphilis: focusing on emerging clinical strategies
and preclinical models[J]. J Transl Med. 2023,21(1):917.
[11]Chad A Brautigam, Ranjit K Deka, Wei Z Liu, et
al.Insights into the potential function and membrane organization
of the TP0435 (Tp17) lipoprotein from Treponema pallidum
derived from structural and biophysical analyses[J]. Protein Sci.
2015,24(1):11-9.
[12]Lorenzo Giacani, Stephanie L Brandt, Wujian Ke, et
al.Transcription of TP0126, Treponema pallidum putative OmpW
homolog, is regulated by the length of a homopolymeric guanosine
repeat[J]. Infect Immun. 2015,83(6):2275-2289.
[13]Austin M Haynes, Charmie Godornes, Wujian Ke, et al.
Evaluation of the Protective Ability of the Treponema pallidum
subsp. pallidum Tp0126 OmpW Homolog in the Rabbit Model of
Syphilis[J]. Infect Immun. 2019,87(8):e00323-19.
[14]Rui-Li Zhang, Qian-Qiu Wang, Li-Jia Yang. Chemerin
induced by Treponema pallidum predicted membrane protein
Tp0965 mediates the activation of endothelial cell via MAPK
signaling pathway[J]. J Cell Biochem. 2019,20(12):19621-19634.
[15]Matthew McKevitt, Mary Beth Brinkman, Melanie
McLoughlin, et al.Genome scale identification of Treponema
pallidum antigens[J]. Infect Immun. 2005,73(7):4445-4450.
[16]Rui-Li Zhang, Jing-Ping Zhang, Qian-Qiu Wang.
Recombinant Treponema pallidum protein Tp0965 activates
endothelial cells and increases the permeability of endothelial cell
monolayer[J]. PLoS One. 2014,9(12):e115134.
[17]A V Runina, G L Katunin, M A Filippova, et al.
Immunochip for Syphilis Serodiagnostics with the Use of Extended
Array of Treponema pallidum Recombinant Antigens.Bull Exp
Biol Med[J]. 2018,165(6):767-771.
[18]Mary Beth Brinkman, Matthew McKevitt, Melanie
McLoughlin, et al. Reactivity of antibodies from syphilis patients to
a protein array representing the Treponema pallidum proteome[J].
J Clin Microbiol[J]. 2006,44(3):888-891.
[19]Man Xu, Yafeng Xie, Chuanhao Jiang, et al. A novel
ELISA using a recombinant outer membrane protein, rTp0663, as
the antigen for serological diagnosis of syphilis[J]. Int J Infect Dis.
2016, 43:51-57.
[20]Li Zhang, Meixia Deng, Xiaohong Zhang, et al.
Serological evaluation of antigen Tp0693 for diagnosis of
syphilis[J]. Exp Ther Med. 2017,14(5):4729-4736.
[21]Philipp P Bosshard. Usefulness of IgM-specific
enzyme immunoassays for serodiagnosis of syphilis: comparative
evaluation of three different assays. Comparative Study[J]. J Infect.
2013,67(1):35-42.
[22]Vitomir Djokic, Lorenzo Giacani, Nikhat Parveen.
Analysis of host cell binding specificity mediated by the Tp0136
adhesin of the syphilis agent Treponema pallidum subsp. Pallidum.
PLoS Negl Trop Dis[J]. 2019,13(5):e0007401.
[23]Caroline E Cameron, Elizabeth L Brown, Janelle M
Y Kuroiwa, et al. Treponema pallidum fibronectin-binding
proteins[J]. J Bacteriol. 2004,186(20):7019-7022.
[24]Wujian Ke, Barbara J Molini, Sheila A Lukehart, et
al.Treponema pallidum subsp. pallidum TP0136 protein is
heterogeneous among isolates and binds cellular and plasma
fibronectin via its NH2-terminal end[J]. PLoS Negl Trop Dis.
2015,9(3):e0003662.
[25]Mary Beth Brinkman , Melanie A McGill, Jonas
Pettersson, et al. A novel Treponema pallidum antigen, TP0136, is
an outer membrane protein that binds human fibronectin[J]. Infect
Immun. 2008,76(5):1848-1857.
[26]Caroline E Cameron. Syphilis Vaccine Development:
Requirements, Challenges, and Opportunities[J]. Sex Transm Dis.
2018,45(9S Suppl 1):S17-S19.
[27]Simon Houston, Rebecca Hof, Teresa Francescutti, et
al.Bifunctional role of the Treponema pallidum extracellular matrix
binding adhesin Tp0751[J]. Infect Immun. 2011,9(3):1386-1398.
[28]Simon Houston, Rebecca Hof, Lisa Honeyman, et al.
Activation and proteolytic activity of the Treponema pallidum
metalloprotease, pallilysin[J]. PLoS Pathog. 2012;8(7):e1002822.
[29]Michelle L Parker, Simon Houston, Helena Pětrošová,
et al. The Structure of Treponema pallidum Tp0751 (Pallilysin)
Reveals a Non-canonical Lipocalin Fold That Mediates Adhesion
to Extracellular Matrix Components and Interactions with Host
Cells[J]. PLoS Pathog. 2016,12(9):e1005919.
[30]Karen V Lithgow, Rebecca Hof, Charmaine Wetherell,
et al. A defined syphilis vaccine candidate inhibits dissemination
of Treponema pallidum subspecies pallidum[J]. Nat Commun.
2017,8:14273.
[31]Nikhat Parveen, Mark C Fernandez, Austin M
Haynes, et al.Non-pathogenic Borrelia burgdorferi expressing
Treponema pallidum TprK and Tp0435 antigens as a novel
approach to evaluate syphilis vaccine candidates[J]. Vaccine.
2019,37(13):1807-1818.
[32]Dan Liu, Man-Li Tong, Xi Luo, et al. Profile of the
tprK gene in primary syphilis patients based on next-generation
sequencing[J].PLoS Negl Trop Dis. 2019,13(2):e0006855.
[33]Rebecca E LaFond, Barbara J Molini, Wesley C
Van Voorhis, et al. Antigenic variation of TprK V regions
abrogates specific antibody binding in syphilis[J]. Infect Immun.
2006,74(11):6244-6251.
[34]Tara B Reid, Barbara J Molini, Mark C Fernandez, et al.
Antigenic variation of TprK facilitates development of secondary
syphilis[J]. Infect Immun. 2014,82(12):4959-4967.
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