Mannose-Binding Lectin Binds to a Range of Clinically Relevant Microorganisms and Promotes Complement Deposition

  • Olaf Neth
    <!--label omitted: 1-->Immunobiology Unit, Institute of Child Health, University College London,1 and
  • Dominic L. Jack
    <!--label omitted: 1-->Immunobiology Unit, Institute of Child Health, University College London,1 and
  • Alister W. Dodds
    <!--label omitted: 2-->Immunochemistry Unit, Medical Research Council, Oxford,2 United Kingdom
  • Helen Holzel
    <!--label omitted: 3-->Department of Microbiology, Great Ormond Street Hospital for Children,3 NHS Trust, London, and
  • Nigel J. Klein
    <!--label omitted: 1-->Immunobiology Unit, Institute of Child Health, University College London,1 and
  • Malcolm W. Turner
    <!--label omitted: 1-->Immunobiology Unit, Institute of Child Health, University College London,1 and

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<jats:title>ABSTRACT</jats:title><jats:p>Mannose-binding lectin (MBL) is a collagenous serum lectin believed to be of importance in innate immunity. Genetically determined low levels of the protein are known to predispose to infections. In this study the binding of purified MBL to pathogens isolated from immunocompromised children was investigated by flow cytometry. Diverse<jats:italic>Candida</jats:italic>species,<jats:italic>Aspergillus fumigatus</jats:italic>,<jats:italic>Staphylococcus aureus</jats:italic>, and beta-hemolytic group A streptococci exhibited strong binding of MBL, whereas<jats:italic>Escherichia coli</jats:italic>,<jats:italic>Klebsiella</jats:italic>species, and<jats:italic>Haemophilus influenzae</jats:italic>type b were characterized by heterogeneous binding patterns. In contrast, beta-hemolytic group B streptococci,<jats:italic>Streptococcus pneumoniae</jats:italic>, and<jats:italic>Staphylococcus epidermidis</jats:italic>showed low levels of binding. Bound MBL was able to promote C4 deposition in a concentration-dependent manner. We conclude that MBL may be of importance in first-line immune defense against several important pathogens.</jats:p>

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