Variation in lipid A structure in the pathogenic yersiniae

被引:220
作者
Rebeil, R
Ernst, RK
Gowen, BB
Miller, SI
Hinnebusch, BJ
机构
[1] NIAID, Lab Human Bacterial Pathogenesis, Rocky Mt Labs, NIH, Hamilton, MT 59840 USA
[2] Univ Washington, Dept Med, Seattle, WA 98195 USA
[3] Univ Washington, Dept Microbiol, Seattle, WA 98195 USA
[4] Univ Washington, Dept Genome Sci, Seattle, WA 98195 USA
关键词
D O I
10.1111/j.1365-2958.2004.04059.x
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
Important pathogens in the genus Yersinia include the plague bacillus Yersinia pestis and two enteropathogenic species, Yersinia pseudotuberculosis and Yersinia enterocolitica. A shift in growth temperature induced changes in the number and type of acyl groups on the lipid A of all three species. After growth at 37degreesC, Y. pestis lipopolysaccharide (LPS) contained the tetra-acylated lipid IVA and smaller amounts of lipid IVA modified with C10 or C12 acyl groups, Y. pseudotuberculosis contained the same forms as part of a more heterogeneous population in which lipid IVA modified with C16:0 predominated, and Y. enterocolitica produced a unique tetra-acylated lipid A. When grown at 21degreesC, however, the three yersiniae synthesized LPS containing predominantly hexa-acylated lipid A. This more complex lipid A stimulated human monocytes to secrete tumour necrosis factor-alpha, whereas the lipid A synthesized by the three species at 37degreesC did not. The Y. pestis phoP gene was required for aminoarabinose modification of lipid A, but not for the temperature-dependent acylation changes. The results suggest that the production of a less immunostimulatory form of LPS upon entry into the mammalian host is a conserved pathogenesis mechanism in the genus Yersinia, and that species-specific lipid A forms may be important for life cycle and pathogenicity differences.
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页码:1363 / 1373
页数:11
相关论文
共 56 条
[1]   Yersinia pestis, the cause of plague, is a recently emerged clone of Yersinia pseudotuberculosis [J].
Achtman, M ;
Zurth, K ;
Morelli, C ;
Torrea, G ;
Guiyoule, A ;
Carniel, E .
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 1999, 96 (24) :14043-14048
[2]   Novel variation of lipid A structures in strains of different Yersinia species [J].
Aussel, L ;
Thérisod, H ;
Karibian, D ;
Perry, MB ;
Bruneteau, M ;
Caroff, M .
FEBS LETTERS, 2000, 465 (01) :87-92
[3]   Pathogenic Yersinia enterocolitica strains increase the outer membrane permeability in response to environmental stimuli by modulating lipopolysaccharide fluidity and lipid A structure [J].
Bengoechea, JA ;
Brandenburg, K ;
Arraiza, MD ;
Seydel, U ;
Skurnik, M ;
Moriyón, I .
INFECTION AND IMMUNITY, 2003, 71 (04) :2014-2021
[4]   Yersinia pseudotuberculosis and Yersinia pestis show increased outer membrane permeability to hydrophobic agents which correlates with lipopolysaccharide acyl-chain fluidity [J].
Bengoechea, JA ;
Brandenburg, K ;
Seydel, U ;
Díaz, R ;
Moriyón, I .
MICROBIOLOGY-UK, 1998, 144 :1517-1526
[5]   Tlr4: central component of the sole mammalian LPS sensor [J].
Beutler, B .
CURRENT OPINION IN IMMUNOLOGY, 2000, 12 (01) :20-26
[6]   Transfer of palmitate from phospholipids to lipid A in outer membranes of Gram-negative bacteria [J].
Bishop, RE ;
Gibbons, HS ;
Guina, T ;
Trent, MS ;
Miller, SI ;
Raetz, CRH .
EMBO JOURNAL, 2000, 19 (19) :5071-5080
[7]   LIPOPOLYSACCHARIDES FROM A SLIGHTLY VIRULENT-STRAIN OF YERSINIA-PESTIS [J].
BORDET, C ;
BRUNETEAU, M ;
MICHEL, G .
EUROPEAN JOURNAL OF BIOCHEMISTRY, 1977, 79 (02) :443-449
[8]  
BROZEK KA, 1989, J BIOL CHEM, V264, P6956
[9]   STRUCTURAL CHARACTERIZATION OF THE LIPID-A OF BORDETELLA-PERTUSSIS 1414-ENDOTOXIN [J].
CAROFF, M ;
DEPRUN, C ;
RICHARDS, JC ;
KARIBIAN, D .
JOURNAL OF BACTERIOLOGY, 1994, 176 (16) :5156-5159
[10]   DETERGENT-ACCELERATED HYDROLYSIS OF BACTERIAL-ENDOTOXINS AND DETERMINATION OF THE ANOMERIC CONFIGURATION OF THE GLYCOSYL PHOSPHATE PRESENT IN THE ISOLATED LIPID-A FRAGMENT OF THE BORDETELLA-PERTUSSIS ENDOTOXIN [J].
CAROFF, M ;
TACKEN, A ;
SZABO, L .
CARBOHYDRATE RESEARCH, 1988, 175 (02) :273-282