The C-terminus of factor H: Monoclonal antibodies inhibit heparin binding and identify epitopes common to factor H and factor-H related proteins

Prodinger, Wolfgang M.; Hellwage, Jens; Spruth, Martin; Dierich, Manfred P.; Zipfel, Peter F.

doi:10.1016/s0161-5890(98)90782-9

Cited by 26 publications

(38 citation statements)

References 19 publications

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“…Currently, the biological functions of FHR-1 are unknown. FHR-1 has a plasma concentration of approximately 20-50 mg/ml, is a constituent of lipoprotein particles, and binds heparin and the central complement components C3b and C3d (Skerka et al, 1991;Wright, 1996, 2000;Prodinger et al, 1998;Zipfel et al, 1999;Majno, 2003).…”

Section: Resultsmentioning

confidence: 99%

“…Human serum (diluted 1:100), FHR-1 or factor H (Calbiochem, Darmstadt, Germany) were added to the wells and incubated overnight at 4 1C. After addition of SCR 1-4 antiserum (Ku¨hn et al, 1995) or mAb VIG8 (Prodinger et al, 1998) for 2 h at room temperature, protein complexes were identified using secondary HRPcoupled antisera. The reaction was developed with 1,2-phenylenediamine dihydrochloride (OPD) (DakoCytomation, Glostrup, Denmark), and the absorbency was measured at 490 nm.…”

Section: Elisamentioning

confidence: 99%

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FHR-1, an additional human plasma protein, binds to complement regulator-acquiring surface proteins of Borrelia burgdorferi

Haupt¹,

Kraiczy²,

Wallich³

et al. 2008

International Journal of Medical Microbiology

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Section: Resultsmentioning

confidence: 99%

Section: Elisamentioning

confidence: 99%

FHR-1, an additional human plasma protein, binds to complement regulator-acquiring surface proteins of Borrelia burgdorferi

Haupt¹,

Kraiczy²,

Wallich³

et al. 2008

International Journal of Medical Microbiology

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“…1a) [11][12][13][14]. Similarly, purified patient-derived autoantibodies block surface binding of Factor H and reduce the protective capacity of Factor H on the cell surface.…”

Section: Autoantibodies To Factor H-mode Of Actionmentioning

confidence: 99%

DEAP-HUS: Deficiency of CFHR plasma proteins and autoantibody-positive form of hemolytic uremic syndrome

et al. 2010

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DEAP-HUS [Deficiency of CFHR (complement factor H-related) plasma proteins and Autoantibody Positive form of Hemolytic Uremic Syndrome] represents a novel subtype of hemolytic uremic syndrome (HUS) with unique characteristics. It affects children and requires special clinical attention in terms of diagnosis and therapy. DEAP-HUS and other atypical forms of HUS share common features, such as microangiopathic hemolytic anemia, acute renal failure, and thrombocytopenia. However, DEAP-HUS has the unique combination of an acquired factor in the form of autoantibodies to the complement inhibitor Factor H and a genetic factor which, in most cases, is the chromosomal deletion of a 84-kbp fragment within human chromosome 1 that results in the absence of the CFHR1 and CFHR3 proteins in plasma. Special attention is required to diagnose and treat DEAP-HUS patients. Most patients show a favorable response to the reduction of autoantibody titers by either plasma therapy, steroid treatment, and/or immunosuppression. In addition, in those DEAP-HUS patients with end-stage renal disease, the reduction of autoantibody titers prior to transplantation is expected to prevent post-transplant disease recurrence by aiming for full complement control at the endothelial cell surface in order to minimize adverse complement and immune reactions.

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“…However, binding of factor H to adhesins via its carboxy-terminus uncoils the protein, which permits interactions between SCR-7 and its ligands (Aslam and Perkins, 2001;Oppermann et al, 2006). Presumably due to the structure of factor H in solution, the carboxy-terminal SCRs provide initial binding of factor H to mammalian cells (Prodinger et al, 1998;Perkins and Goodship, 2002;Jokiranta et al, 2005;Oppermann et al, 2006;Jo´szi et al, 2007). By analogy, Erp proteins may provide initial contact between the bacteria and factor H through SCR-20, causing the structure of factor H to open up and permit BbCRASPs-1 and/or -2 to bind the host protein more tightly via SCR-7.…”

Section: Article In Pressmentioning

confidence: 99%

Lyme borreliosis spirochete Erp proteins, their known host ligands, and potential roles in mammalian infection

Brissette

Cooley

Burns

et al. 2008

International Journal of Medical Microbiology

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Lyme borreliae naturally maintain numerous distinct DNA elements of the cp32 family, each of which carries a mono- or bicistronic erp locus. The encoded Erp proteins are surface-exposed outer membrane lipoproteins that are produced at high levels during mammalian infection but largely repressed during colonization of vector ticks. Recent studies have revealed that some Erp proteins can serve as bacterial adhesins, binding host proteins such as the complement regulator factor H and the extracellular matrix component laminin. These results suggest that Erp proteins play roles in multiple aspects of mammalian infection.

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The C-terminus of factor H: Monoclonal antibodies inhibit heparin binding and identify epitopes common to factor H and factor-H related proteins

Cited by 26 publications

References 19 publications

FHR-1, an additional human plasma protein, binds to complement regulator-acquiring surface proteins of Borrelia burgdorferi

FHR-1, an additional human plasma protein, binds to complement regulator-acquiring surface proteins of Borrelia burgdorferi

DEAP-HUS: Deficiency of CFHR plasma proteins and autoantibody-positive form of hemolytic uremic syndrome

Lyme borreliosis spirochete Erp proteins, their known host ligands, and potential roles in mammalian infection

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