SUMMARYMannan-binding protein (MBP), a calcium-dependent plasma lectin, may play a role in the innate defence against microorganisms. After binding lo carbohydrate structures at the bacterial surface, MBP activates the classical pathway of the complement system. To investigate the binding capacity of MBP to various bacteria associated with meningitis, an assay was developed to study the binding of MBP to bacteria grown in a semisynthctic lluid culture medium. Salmonella montevideo (containing a mannose-rich lipopolysaceharide (EPS)), used as a positive control strain, showed binding of radioiabclled MBP at a level of 80% compared with binding of MBP to zymosan. Binding of labelled MBP to Salm. monievideo was time-dependent, temperaturedependent and saturablc. The binding, was inhibited by unlabelled MBP., by mannose and by Nacetyl-ij-glucosamine. Among bacterial pathogens often found to cause meningitis, a wide range of MBP binding capacities could be determined. The encapsulated Neisseriu meningitidis (representatives from 11 serogroups other than group A were included: n ~ 22), N. mucosa {n = \), iUicmophilus mfiuenzae type b \n = 10) and Streptococcus agalactiae [n = 5) had a low MBP binding capacity of21-7% (95% confidence interval (Cl)3'3 4i)\%). Escheriehia coliK\ (« = 11).Strep, suis {n = 5), Strep, pneumoniae (n = 10) and N. meningitidis scrogroup A (n = 2) showed intermediate MBP binding capacity of 58-4% (95% Cl 40-0-76 8%). A third group consisting of non-encapsulated Listeria monocytogenes (rt = 11), non-encapsulated H. injluenzae (n = 2), nonencapsulated N. meningitidis (n = 2), N. cinera {n = \) and N. .subflava {n = \) strains had a high MBP binding capacity of 875% (95% C! 62'5 112 5%). The majority of encapsulated pathogens causing bacterial meningitis seem to have a rather low MBP binding capacity.