Development, characterization, and functional activity of a panel of specific monoclonal antibodies to inner core lipopolysaccharide epitopes in Neisseria meningitidis. 2004

Margaret Anne J Gidney, and Joyce S Plested, and Suzanne Lacelle, and Philip A Coull, and J Claire Wright, and Katherine Makepeace, and Jean-Robert Brisson, and Andrew D Cox, and E Richard Moxon, and James C Richards
Institute for Biological Sciences, National Research Council, Ottawa, ON, K1A OR6, Canada. margaretanne.gidney@nrc-cnrc.gc.ca

A panel of six murine monoclonal antibodies (MAbs) recognizing inner core lipopolysaccharide (LPS) epitopes of Neisseria meningitidis was prepared and characterized in order to determine the diversity of inner core LPS glycoforms among disease and carrier isolates. Two of these MAbs, L2-16 (immunoglobulin G2b [IgG2b]) and LPT3-1 (IgG2a), together with a third, previously described MAb, L3B5 (IgG3), showed reactivity, either individually or in combination, with all except 3 of 143 disease and carriage isolates (125 of 126 strains from blood, cerebrospinal fluid, or skin biopsy samples and 15 of 17 from nasopharyngeal cultures). MAbs L3B5, L2-16, and LPT3-1 were further characterized in an indirect immunofluorescence assay. All three MAbs bound to the bacterial cell surface, findings that correlated strongly with whole-cell enzyme-linked immunosorbent assay and immunodot blots. However, in contrast to our findings with L3B5, cell surface binding of L2-16 or LPT 3-1 did not correlate with functional activity as determined by bactericidal or infant rat passive protection assays against wild-type N. meningitidis strains. These findings are provocative with respect to the requirements for protective activity of antibodies and the development of inner core LPS vaccines against invasive meningococcal disease.

UI MeSH Term Description Entries
D008070 Lipopolysaccharides Lipid-containing polysaccharides which are endotoxins and important group-specific antigens. They are often derived from the cell wall of gram-negative bacteria and induce immunoglobulin secretion. The lipopolysaccharide molecule consists of three parts: LIPID A, core polysaccharide, and O-specific chains (O ANTIGENS). When derived from Escherichia coli, lipopolysaccharides serve as polyclonal B-cell mitogens commonly used in laboratory immunology. (From Dorland, 28th ed) Lipopolysaccharide,Lipoglycans
D008585 Meningitis, Meningococcal A fulminant infection of the meninges and subarachnoid fluid by the bacterium NEISSERIA MENINGITIDIS, producing diffuse inflammation and peri-meningeal venous thromboses. Clinical manifestations include FEVER, nuchal rigidity, SEIZURES, severe HEADACHE, petechial rash, stupor, focal neurologic deficits, HYDROCEPHALUS, and COMA. The organism is usually transmitted via nasopharyngeal secretions and is a leading cause of meningitis in children and young adults. Organisms from Neisseria meningitidis serogroups A, B, C, Y, and W-135 have been reported to cause meningitis. (From Adams et al., Principles of Neurology, 6th ed, pp689-701; Curr Opin Pediatr 1998 Feb;10(1):13-8) Meningitis, Neisseria,Neisseria Meningitis,Meningitis, Meningococcal, Serogroup A,Meningitis, Meningococcal, Serogroup B,Meningitis, Meningococcal, Serogroup C,Meningitis, Meningococcal, Serogroup W-135,Meningitis, Meningococcal, Serogroup W135,Meningitis, Meningococcal, Serogroup Y,Meningitis, Meningococcic,Meningococcal Meningitis, Serogroup A,Meningococcal Meningitis, Serogroup B,Meningococcal Meningitis, Serogroup C,Meningococcal Meningitis, Serogroup W-135,Meningococcal Meningitis, Serogroup W135,Meningococcal Meningitis, Serogroup Y,Serogroup A Meningococcal Meningitis,Serogroup B Meningococcal Meningitis,Serogroup C Meningococcal Meningitis,Serogroup W-135, Meningococcal Meningitis,Serogroup W135, Meningococcal Meningitis,Serogroup Y, Meningococcal Meningitis,Meningococcal Meningitis,Meningococcal Meningitis, Serogroup W 135,Neisseria Meningitides,Serogroup W 135, Meningococcal Meningitis
D008958 Models, Molecular Models used experimentally or theoretically to study molecular shape, electronic properties, or interactions; includes analogous molecules, computer-generated graphics, and mechanical structures. Molecular Models,Model, Molecular,Molecular Model
D009895 Opsonin Proteins Proteins that bind to particles and cells to increase susceptibility to PHAGOCYTOSIS, especially ANTIBODIES bound to EPITOPES that attach to FC RECEPTORS. COMPLEMENT C3B may also participate. Opsonin,Opsonin Protein,Opsonins,Protein, Opsonin
D010587 Phagocytosis The engulfing and degradation of microorganisms; other cells that are dead, dying, or pathogenic; and foreign particles by phagocytic cells (PHAGOCYTES). Phagocytoses
D001770 Blood Bactericidal Activity The natural bactericidal property of BLOOD due to normally occurring antibacterial substances such as beta lysin, leukin, etc. This activity needs to be distinguished from the bactericidal activity contained in a patient's serum as a result of antimicrobial therapy, which is measured by a SERUM BACTERICIDAL TEST. Activities, Blood Bactericidal,Activity, Blood Bactericidal,Bactericidal Activities, Blood,Bactericidal Activity, Blood,Blood Bactericidal Activities
D003429 Cross Reactions Serological reactions in which an antiserum against one antigen reacts with a non-identical but closely related antigen. Cross Reaction,Reaction, Cross,Reactions, Cross
D004797 Enzyme-Linked Immunosorbent Assay An immunoassay utilizing an antibody labeled with an enzyme marker such as horseradish peroxidase. While either the enzyme or the antibody is bound to an immunosorbent substrate, they both retain their biologic activity; the change in enzyme activity as a result of the enzyme-antibody-antigen reaction is proportional to the concentration of the antigen and can be measured spectrophotometrically or with the naked eye. Many variations of the method have been developed. ELISA,Assay, Enzyme-Linked Immunosorbent,Assays, Enzyme-Linked Immunosorbent,Enzyme Linked Immunosorbent Assay,Enzyme-Linked Immunosorbent Assays,Immunosorbent Assay, Enzyme-Linked,Immunosorbent Assays, Enzyme-Linked
D006801 Humans Members of the species Homo sapiens. Homo sapiens,Man (Taxonomy),Human,Man, Modern,Modern Man
D000818 Animals Unicellular or multicellular, heterotrophic organisms, that have sensation and the power of voluntary movement. Under the older five kingdom paradigm, Animalia was one of the kingdoms. Under the modern three domain model, Animalia represents one of the many groups in the domain EUKARYOTA. Animal,Metazoa,Animalia

Related Publications

Margaret Anne J Gidney, and Joyce S Plested, and Suzanne Lacelle, and Philip A Coull, and J Claire Wright, and Katherine Makepeace, and Jean-Robert Brisson, and Andrew D Cox, and E Richard Moxon, and James C Richards
December 1983, Infection and immunity,
Margaret Anne J Gidney, and Joyce S Plested, and Suzanne Lacelle, and Philip A Coull, and J Claire Wright, and Katherine Makepeace, and Jean-Robert Brisson, and Andrew D Cox, and E Richard Moxon, and James C Richards
March 2002, Infection and immunity,
Margaret Anne J Gidney, and Joyce S Plested, and Suzanne Lacelle, and Philip A Coull, and J Claire Wright, and Katherine Makepeace, and Jean-Robert Brisson, and Andrew D Cox, and E Richard Moxon, and James C Richards
September 2002, European journal of biochemistry,
Margaret Anne J Gidney, and Joyce S Plested, and Suzanne Lacelle, and Philip A Coull, and J Claire Wright, and Katherine Makepeace, and Jean-Robert Brisson, and Andrew D Cox, and E Richard Moxon, and James C Richards
January 2017, PloS one,
Margaret Anne J Gidney, and Joyce S Plested, and Suzanne Lacelle, and Philip A Coull, and J Claire Wright, and Katherine Makepeace, and Jean-Robert Brisson, and Andrew D Cox, and E Richard Moxon, and James C Richards
January 2010, Journal of bacteriology,
Margaret Anne J Gidney, and Joyce S Plested, and Suzanne Lacelle, and Philip A Coull, and J Claire Wright, and Katherine Makepeace, and Jean-Robert Brisson, and Andrew D Cox, and E Richard Moxon, and James C Richards
November 1996, Brazilian journal of medical and biological research = Revista brasileira de pesquisas medicas e biologicas,
Margaret Anne J Gidney, and Joyce S Plested, and Suzanne Lacelle, and Philip A Coull, and J Claire Wright, and Katherine Makepeace, and Jean-Robert Brisson, and Andrew D Cox, and E Richard Moxon, and James C Richards
October 1990, Zhurnal mikrobiologii, epidemiologii i immunobiologii,
Margaret Anne J Gidney, and Joyce S Plested, and Suzanne Lacelle, and Philip A Coull, and J Claire Wright, and Katherine Makepeace, and Jean-Robert Brisson, and Andrew D Cox, and E Richard Moxon, and James C Richards
October 2004, Journal of bacteriology,
Margaret Anne J Gidney, and Joyce S Plested, and Suzanne Lacelle, and Philip A Coull, and J Claire Wright, and Katherine Makepeace, and Jean-Robert Brisson, and Andrew D Cox, and E Richard Moxon, and James C Richards
August 1992, Journal of clinical microbiology,
Margaret Anne J Gidney, and Joyce S Plested, and Suzanne Lacelle, and Philip A Coull, and J Claire Wright, and Katherine Makepeace, and Jean-Robert Brisson, and Andrew D Cox, and E Richard Moxon, and James C Richards
December 1981, Infection and immunity,
Copied contents to your clipboard!