The interaction between RTX toxins and target cells

被引:213
作者
Lally, ET [1 ]
Hill, RB
Kieba, LR
Korostoff, J
机构
[1] Univ Penn, Sch Med, Leon Levy Res Ctr Oral Biol, Philadelphia, PA 19104 USA
[2] Univ Penn, Sch Med, Dept Biochem & Biophys, Philadelphia, PA 19104 USA
关键词
D O I
10.1016/S0966-842X(99)01530-9
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
RTX toxins are important virulence factors produced by a wide range of Gram-negative bacteria. They fall into two categories: the hemolysins, which affect a variety of cell types, and the leukotoxins, which are cell-type- and species-specific. These toxins offer interesting models for targeting, insertion and translocation of aqueous proteins into lipid membranes.
引用
收藏
页码:356 / 361
页数:6
相关论文
共 52 条
  • [1] Reversible adsorption and nonreversible insertion of Escherichia coli alpha-hemolysin into lipid bilayers
    Bakas, L
    Ostolaza, H
    Vaz, WLC
    Goni, FM
    [J]. BIOPHYSICAL JOURNAL, 1996, 71 (04) : 1869 - 1876
  • [2] ESCHERICHIA-COLI HEMOLYSIN MAY DAMAGE TARGET-CELL MEMBRANES BY GENERATING TRANSMEMBRANE PORES
    BHAKDI, S
    MACKMAN, N
    NICAUD, JM
    HOLLAND, IB
    [J]. INFECTION AND IMMUNITY, 1986, 52 (01) : 63 - 69
  • [3] ROLES OF LIPID MODIFICATIONS OF TRANSDUCIN SUBUNITS IN THEIR GDP-DEPENDENT ASSOCIATION AND MEMBRANE-BINDING
    BIGAY, J
    FAUROBERT, E
    FRANCO, M
    CHABRE, M
    [J]. BIOCHEMISTRY, 1994, 33 (47) : 14081 - 14090
  • [4] CIRCULATING INTEGRINS - ALPHA-5-BETA-1, ALPHA-6-BETA-4 AND MAC-1, BUT NOT ALPHA-3-BETA-1, ALPHA-4-BETA-1 OR LFA-1
    BRETSCHER, MS
    [J]. EMBO JOURNAL, 1992, 11 (02) : 405 - 410
  • [5] ESCHERICHIA-COLI ALPHA-HEMOLYSIN - CHARACTERISTICS AND PROBABLE ROLE IN PATHOGENICITY
    CAVALIERI, SJ
    BOHACH, GA
    SNYDER, IS
    [J]. MICROBIOLOGICAL REVIEWS, 1984, 48 (04) : 326 - 343
  • [6] THE CRYSTAL-STRUCTURE OF DIPHTHERIA-TOXIN
    CHOE, S
    BENNETT, MJ
    FUJII, G
    CURMI, PMG
    KANTARDJIEFF, KA
    COLLIER, RJ
    EISENBERG, D
    [J]. NATURE, 1992, 357 (6375) : 216 - 222
  • [7] DELETION ANALYSIS RESOLVES CELL-BINDING AND LYTIC DOMAINS OF THE PASTEURELLA LEUKOTOXIN
    CRUZ, WT
    YOUNG, R
    CHANG, YF
    STRUCK, DK
    [J]. MOLECULAR MICROBIOLOGY, 1990, 4 (11) : 1933 - 1939
  • [8] A FAMILY OF EXTRACYTOPLASMIC PROTEINS THAT ALLOW TRANSPORT OF LARGE MOLECULES ACROSS THE OUTER MEMBRANES OF GRAM-NEGATIVE BACTERIA
    DINH, T
    PAULSEN, IT
    SAIER, MH
    [J]. JOURNAL OF BACTERIOLOGY, 1994, 176 (13) : 3825 - 3831
  • [9] A mechanism for toxin insertion into membranes is suggested by the crystal structure of the channel-forming domain of colicin E1
    Elkins, P
    Bunker, A
    Cramer, WA
    Stauffacher, CV
    [J]. STRUCTURE, 1997, 5 (03) : 443 - 458
  • [10] NUCLEOTIDE-SEQUENCE OF AN ESCHERICHIA-COLI CHROMOSOMAL HEMOLYSIN
    FELMLEE, T
    PELLETT, S
    WELCH, RA
    [J]. JOURNAL OF BACTERIOLOGY, 1985, 163 (01) : 94 - 105