Complement evasion strategies of pathogens-Acquisition of inhibitors and beyond

被引:166
作者
Blom, Anna M. [1 ]
Hallstrom, Teresia [1 ]
Riesbeck, Kristian [1 ]
机构
[1] Lund Univ, Div Med Prot Chem, Dept Lab Med, Univ Hosp Malmo,Wallenberg Lab, SE-20502 Malmo, Sweden
关键词
Complement; Serum resistance; C4b-binding protein; Factor H; Vitronectin; C3; Bacterial proteases; HUMAN C4B-BINDING PROTEIN; STREPTOCOCCAL-M-PROTEIN; C4B BINDING-PROTEIN; HUMAN-FACTOR-H; MEDIATES SERUM RESISTANCE; GROUP-A STREPTOCOCCI; ESCHERICHIA-COLI K1; REGULATOR FACTOR-H; NEISSERIA-GONORRHOEAE; BORRELIA-BURGDORFERI;
D O I
10.1016/j.molimm.2009.04.025
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
Activation of the complement system and resulting opsonisation with Ob are key events of the innate immune defense against infections. However, a wide variety of bacterial pathogens subvert complement attack by binding host complement inhibitors such as C4b-binding protein, factor H and vitronectin, which results in diminished opsonophagocytosis and killing of bacteria by lysis. Another widely used strategy is production of proteases, which can effectively degrade crucial complement components. Furthermore, bacterial pathogens such as Moraxella catarrhalis and Staphylococcus aureus capture and incapacitate the key complement component C3. The current review describes examples of these three strategies. Targeting binding sites for complement inhibitors on bacterial surfaces and complement-degrading proteases with vaccine-induced antibodies may be used to enhance a common vaccine design strategy that depends on the generation of complement-dependent bactericidal and opsonophagocytic antibody activities. (C) 2009 Elsevier Ltd. All rights reserved.
引用
收藏
页码:2808 / 2817
页数:10
相关论文
共 127 条
[1]  
Accardo P, 1996, J IMMUNOL, V157, P4935
[2]   BINDING-PROPERTIES OF PROTEIN ARP, A BACTERIAL IGA-RECEPTOR [J].
AKERSTROM, B ;
LINDQVIST, A ;
LINDAHL, G .
MOLECULAR IMMUNOLOGY, 1991, 28 (4-5) :349-357
[3]   Lysine-dependent multipoint binding of the Borrelia burgdorferi virulence factor outer surface protein E to the C terminus of factor H [J].
Alitalo, A ;
Meri, T ;
Chen, T ;
Lankinen, H ;
Cheng, ZZ ;
Jokiranta, TS ;
Seppälä, KJT ;
Lahdenne, P ;
Hefty, PS ;
Akins, DR ;
Meri, S .
JOURNAL OF IMMUNOLOGY, 2004, 172 (10) :6195-6201
[4]   Streptococcal M protein:: Structural studies of the hypervariable region, free and bound to human C4BP [J].
André, I ;
Persson, J ;
Blom, AM ;
Nilsson, H ;
Drakenberg, T ;
Lindahl, G ;
Linse, S .
BIOCHEMISTRY, 2006, 45 (14) :4559-4568
[5]   MODIFICATION BY SIALIC-ACID OF NEISSERIA-GONORRHOEAE LIPOOLIGOSACCHARIDE EPITOPE EXPRESSION IN HUMAN URETHRAL EXUDATES - AN IMMUNOELECTRON MICROSCOPIC ANALYSIS [J].
APICELLA, MA ;
MANDRELL, RE ;
SHERO, M ;
WILSON, ME ;
GRIFFISS, JM ;
BROOKS, GF ;
LAMMEL, C ;
BREEN, JF ;
RICE, PA .
JOURNAL OF INFECTIOUS DISEASES, 1990, 162 (02) :506-512
[6]   ANIMAL-MODELS FOR PATHOGENIC NEISSERIA SPECIES [J].
ARKO, RJ .
CLINICAL MICROBIOLOGY REVIEWS, 1989, 2 :S56-S59
[7]   Binding of vitronectin by the Moraxella catarrhalis UspA2 protein interferes with late stages of the complement cascade [J].
Attia, AS ;
Ram, S ;
Rice, PA ;
Hansen, EJ .
INFECTION AND IMMUNITY, 2006, 74 (03) :1597-1611
[8]   C4B-BINDING PROTEIN, A REGULATORY COMPONENT OF THE CLASSICAL PATHWAY OF COMPLEMENT, IS AN ACUTE-PHASE PROTEIN AND IS ELEVATED IN SYSTEMIC LUPUS-ERYTHEMATOSUS [J].
BARNUM, SR ;
DAHLBACK, B .
COMPLEMENT AND INFLAMMATION, 1990, 7 (02) :71-77
[9]   Fine antigenic specificity and cooperative bactericidal activity of monoclonal antibodies directed at the meningococcal vaccine candidate factor H-binding protein [J].
Beernink, Peter T. ;
Welsch, Jo Anne ;
Bar-Lev, Michal ;
Koeberling, Oliver ;
Comanducci, Maurizio ;
Granoff, Dan M. .
INFECTION AND IMMUNITY, 2008, 76 (09) :4232-4240
[10]   The opportunistic human pathogenic fungus Aspergillus fumigatus evades the host complement system [J].
Behnsen, Judith ;
Hartmann, Andrea ;
Schmaler, Jeannette ;
Gehrke, Alexander ;
Brakhage, Axel A. ;
Zipfel, Peter F. .
INFECTION AND IMMUNITY, 2008, 76 (02) :820-827