RESEARCH PAPER
Borrelia burgdorferi sensu lato as activators of the complement system in in vitro model
 
More details
Hide details
1
Department of Medical Microbiology, Medical University, Lublin, Poland
 
2
Department of Infectious Diseases, Medical University, Lublin, Poland
 
3
National Institute of Public Health – National Institute of Hygiene, Laboratory of Rickettsiae, Chlamydiae and Spirochaetes, Warsaw, Poland
 
 
Ann Agric Environ Med. 2012;19(4):641-645
 
KEYWORDS
ABSTRACT
Introduction:
The following parameters were analyzed: C5a, which is significant in classical and alternative pathways of the complement system activation, and factor H, the major function of which is to regulate the alternative pathway. Factor H, in the case of Borrelia infection, is combined by CRASPs proteins of spirochetes, and thus prevents C3b molecules from contact with the pathogen, opsonisation and lysis of bacteria.

Material and Methods:
The experimental material in the model for the presented work consisted of whole blood of healthy persons (without the presence of antibodies anti-Borrelia) and persons with clinical symptoms of Lyme disease, which was stimulated with three genospecies of spirochetes recognized as pathogenic in Poland and Europe:B. afzelii, B. burgdorferi s.s and B. garinii.

Results:
The increase in the level of C5a in the experimental model after in vitro stimulation of whole blood with three genospecies Borrelia can be treated as an indicator of an effective activation of the complement’s cascade. The increase in level C5a in the plasma relies on the genospecies and the strongest is for B. garinii. The decrease in the level of factor H, observed after the incubation of whole blood with three genospecies Borrelia, shows that this parameter was included in the spirochetes’ mechanisms acting against factors of the innate immunity system of a host, which prevents lysis of bacteria via the alternative pathway.

Conclusions:
The results obtained on the basis of the in vitro model can be analysed from the aspect of spirochetes’ real contact with a host’s organism during the bite of infected ticks. Despite blocking of the alternative pathway, Borrelia initiate the activation cascade regardless of antibodies via the first contact of a host’s organism with spirochetes, or in accordance with antibodies during the infection or subsequent contact with bacteria.

 
REFERENCES (17)
1.
Brooks Ch, Vuppala SR, Jett AM, Alitalo A, Meri S, Akins DR. Complement regulator-acquiring surface protein1 imparts resistance to human serum in Borrelia burgdorferi. J Immunol. 2005; 175: 3299-3308.
 
2.
Bykowski T, Woodman ME, Cooley AE, Brissette A, Wallich R, Brade V, Kraiczy P, Stevenson B. Borrelia burgdorferi Complement regulator-acquiring surface proteins (BbCRASPs): Expression patterns during the mammal-tick infection cycle. IJMM. 2008; 298(supl 1): 249-256.
 
3.
Krajczy P, Skerka Ch, Kirschfink M, Zipfel PF, Brade V. Mechanism of complement resistance of pathogenic Borrelia burgdorferi isolates. Int Immunopharmacol. 2001; 1: 393-401.
 
4.
Krajczy P, Skerka Ch, Kirschfink M, Zipfel PF, Brade V. Immune evasion of Borrelia burgdorferi: Insufficient killing of the pathogens by complement and antibody. Int J Med Microbiol. 2002; 291(supl 33): 141-146.
 
5.
Krajczy P, Schreiber J, Skerka Ch, Haupt K, Brade V, Weallich R, et al. Assessment of the regions within complement regulator-acquiring surface protein (CRASP)-2 of Borrelia burgdorferi required for interaction with host immune regulators FHL-1 and factor H. Int J Med Microbiol. 2008; 298(supl 1): 268-271.
 
6.
Siegel C, Hallstrom T, Skerka C, Eberhardt H, Uzonyi B, Beckhaus T, et al. Complement factorH-related proteins CFHR2 and CFHR5 represent novel ligands for the infection-associated CRASP protein sof Borrelia burgdorferi. PLoS ONE 5, 10,13519,(2010)http://www.plosone.org/article... (access: 2012.04.20.).
 
7.
Suchonen J, Hartiala K, Tuominen-Gusstafson H, Viljanen MK. Sublethal concentrations of complement can effectively opsonize Borrelia burgdorferi. Scand J Immunol. 2002; 56, 554-560.
 
8.
Singh SK, Girschick, HJ. Molecular survival strategies of the Lyme disease spirochete Borrelia burgdorferi. Lancet Infect Dis. 2004; 4(9): 4575-83.
 
9.
Stanek G, Fingerle V, Hunfeld KP, Jaulhac B, Kaiser R, Krause A, et al. Lyme borreliosis: Clinical case definitions for diagnosis and management in Europe. Clin Microbiol Infect. 2011; 17(1): 69-79.
 
10.
Wilske B, Fingerle V, Schulte-Spechtel U. Microbiological and serological diagnosis of Lyme borreliosis. FEMS Immunol Med Microbiol. 2007; 49(1): 13-21.
 
11.
Pollack RJ, Teleford SR, Spielman A. Standardization of medium for culturing Lyme disease spirochetes. J Clin Microbiol. 1993; 31: 1251-1255.
 
12.
Sprong T, Møller ASW, Bjerre A, Wedege E, Kierulf P, van der Meer JWM, et al. Complement activation and complement-dependent inflammation by Neisseria meningitidis are independent of lipopolsacharide. Infect Immun. 2004; 72(6): 3344-3349.
 
13.
Mollnes TE, Brekke OL, Fung M, Fure H, Christiansen D, Bergseth G, et al. Essentials role of the C5a receptor in E. coli induced oxidative burst and phagocytosis revealed by a novel lepirudin-based human whole blond model of in ammation. Blood . 2002; 100(5): 1869-1877.
 
14.
Barratt-Due A, Thorgersen BE, Linstad JK, Pharo A, Brekke OL, Christiansen D, et al. Selective inhibition of TNF-α or IL1β does not affect E. coli-induced inflammation in human whole blond. Molec Immunol. 2010; 47: 1774-1782.
 
15.
Futoma-Kołoch B., Bugla-Płoskońska G. The efficiency of the bactericidal action of serum raised by complement and lysozyme against bacteria which avoid the immunological response of higher organisms. Postepy Hig Med Dosw. 2009; 63: 471-484.
 
16.
Hofmann H, Wallach R, Lorenz I. Comparison of a new line assai using purified and recombinant antigens with a European lysate blot for serodiagnosis of Lyme borreliosis. IJMM. 2006; 296: 288-290.
 
17.
Klaska I, Nowak JZ. The role of complement in physiology and pathology. Postepy Hig Med Dośw. 2007; 61: 167-177.
 
eISSN:1898-2263
ISSN:1232-1966
Journals System - logo
Scroll to top