Dissecting the structure of LcrV from Yersinia pestis, a truly unique virulence protein

被引:7
|
作者
Nilles, ML [1 ]
机构
[1] Univ N Dakota, Sch Med & Hlth Sci, Dept Microbiol & Immunol, Grand Forks, ND 58203 USA
关键词
D O I
10.1016/j.str.2004.02.026
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
Last month in the February issue, Structure published the crystal structure of LcrV from Yersinia pestis, the infectious agent that causes plague. LcrV activity is essential for disease, and the structure of this protein provides a valuable tool to dissect the nature of its pathogenicity.
引用
收藏
页码:357 / 358
页数:2
相关论文
共 50 条
  • [1] Structure of the Yersinia pestis tip protein LcrV refined to 1.65 Å resolution
    Chaudhury, Sukanya
    Battaile, Kevin P.
    Lovell, Scott
    Plano, Gregory V.
    De Guzman, Roberto N.
    [J]. ACTA CRYSTALLOGRAPHICA SECTION F-STRUCTURAL BIOLOGY COMMUNICATIONS, 2013, 69 : 477 - 481
  • [2] Targeting of LcrV virulence protein from Yersinia pestis to dendritic cells protects mice against pneumonic plague
    Do, Yoonkyung
    Koh, Hyein
    Park, Chae Gyu
    Dudziak, Diana
    Seo, Patrick
    Mehandru, S.
    Choi, Jae-Hoon
    Cheong, Cheolho
    Park, Steven
    Perlin, David S.
    Powell, Bradford S.
    Steinman, Ralph M.
    [J]. EUROPEAN JOURNAL OF IMMUNOLOGY, 2010, 40 (10) : 2791 - 2796
  • [3] Amino acid and structural variability of Yersinia pestis LcrV protein
    Anisimov, Andrey P.
    Dentovskaya, Svetlana V.
    Panfertsev, Evgeniy A.
    Svetoch, Tat'yana E.
    Kopylov, Pavel Kh.
    Segelke, Brent W.
    Zemla, Adam
    Telepnev, Maxim V.
    Motin, Vladimir L.
    [J]. INFECTION GENETICS AND EVOLUTION, 2010, 10 (01) : 137 - 145
  • [4] The weak interaction of LcrV and TLR2 does not contribute to the virulence of Yersinia pestis
    Reithmeier-Rost, D.
    Hill, J.
    Elwin, S. J.
    Williamson, D.
    Dittmann, S.
    Schmid, A.
    Wilharm, G.
    Sing, A.
    [J]. INTERNATIONAL JOURNAL OF MEDICAL MICROBIOLOGY, 2007, 297 : 100 - 100
  • [5] The weak interaction of LcrV and TLR2 does not contribute to the virulence of Yersinia pestis
    Reithmeier-Rost, Dagmar
    Hill, Jim
    Elvin, Stephen J.
    Williamson, Diane
    Dittmann, Svea
    Schmid, Annika
    Wilharm, Gottfried
    Sing, Andreas
    [J]. MICROBES AND INFECTION, 2007, 9 (08) : 997 - 1002
  • [6] Survival protein A is essential for virulence in Yersinia pestis
    Southern, Stephanie J.
    Scott, Andrew E.
    Jenner, Dominic C.
    Ireland, Philip M.
    Norville, Isobel H.
    Sarkar-Tyson, Mitali
    [J]. MICROBIAL PATHOGENESIS, 2016, 92 : 50 - 53
  • [7] Structure-function analysis of the C-terminal domain of LcrV from Yersinia pestis
    Hamad, Mohamad A.
    Nilles, Matthew L.
    [J]. JOURNAL OF BACTERIOLOGY, 2007, 189 (18) : 6734 - 6739
  • [8] Kinetic epitope mapping of monoclonal antibodies raised against the Yersinia pestis virulence factor LcrV
    Read, Thomas
    Olkhov, Rouslan V.
    Williamson, E. Diane
    Shaw, Andrew M.
    [J]. BIOSENSORS & BIOELECTRONICS, 2015, 65 : 47 - 53
  • [9] LcrV of Yersinia pestis enters infected eukaryotic cells by a virulence plasmid-independent mechanism
    Fields, KA
    Straley, SC
    [J]. INFECTION AND IMMUNITY, 1999, 67 (09) : 4801 - 4813
  • [10] Evaluation of the role of LcrV-Toll-Like receptor 2-mediated immunomodulation in the virulence of Yersinia pestis
    Pouliot, Kimberly
    Pan, Ning
    Wang, Shixia
    Lu, Shan
    Lien, Egil
    Goguen, Jon D.
    [J]. INFECTION AND IMMUNITY, 2007, 75 (07) : 3571 - 3580