Martine P. Bos

Additive and synergistic bactericidal activity of antibodies directed against minor outer membrane proteins of Neisseria meningitidis (2007)

Weynants, Vincent E., Feron, Christiane M., Goraj, Karine K., Bos, Martine P., Denoel, Philippe A, Verlant, Vincent G., ...

Neisseria meningitidis serogroup B is a major cause of bacterial meningitis in younger populations. The available vaccines are based on outer membrane vesicles obtained from wild-type strains. In...

Additive and synergistic bactericidal activity of antibodies directed against minor outer membrane proteins of Neisseria meningitidis (2007)

Weynants, Vincent E., Feron, Christiane M., Goraj, Karine K., Bos, Martine P., Denoel, Philippe A, Verlant, Vincent G., ...

Neisseria meningitidis serogroup B is a major cause of bacterial meningitis in younger populations. The available vaccines are based on outer membrane vesicles obtained from wild-type strains. In...

Additive and synergistic bactericidal activity of antibodies directed against minor outer membrane proteins of Neisseria meningitidis (2007)

Weynants, Vincent E., Feron, Christiane M., Goraj, Karine K., Bos, Martine P., Denoel, Philippe A, Verlant, Vincent G., ...

Neisseria meningitidis serogroup B is a major cause of bacterial meningitis in younger populations. The available vaccines are based on outer membrane vesicles obtained from wild-type strains. In...

Additive and synergistic bactericidal activity of antibodies directed against minor outer membrane proteins of Neisseria meningitidis (2007)

Weynants, Vincent E., Feron, Christiane M., Goraj, Karine K., Bos, Martine P., Denoel, Philippe A, Verlant, Vincent G., ...

Neisseria meningitidis serogroup B is a major cause of bacterial meningitis in younger populations. The available vaccines are based on outer membrane vesicles obtained from wild-type strains. In...

Assembly Factor Omp85 Recognizes Its Outer Membrane Protein Substrates by a Species-Specific C-Terminal Motif (2006)

Viviane Robert, Elena B. Volokhina, Freya Senf, Martine P. Bos, Patrick Van Gelder, Jan Tommassen

Integral β-barrel proteins are found in the outer membranes of Gram-negative bacteria, mitochondria, and chloroplasts. The assembly of these proteins requires a proteinaceous apparatus of which...

CD66 receptor specificity exhibited by neisserial Opa variants is controlled by protein determinants in CD66 N-domains

Bos, Martine P., Kuroki, Motomu, Krop-Watorek, Anna, Hogan, Daniel, Belland, Robert J.

Neisseria gonorrhoeae strain MS11 is able to express 11 different opacity (Opa) proteins on its outer surface. A number of these Opa proteins have been shown to function as adhesins through binding...

Carcinoembryonic Antigen Family Receptor Recognition by Gonococcal Opa Proteins Requires Distinct Combinations of Hypervariable Opa Protein Domains

Bos, Martine P., Kao, David, Hogan, Daniel M., Grant, Christopher C. R., Belland, Robert J.

Neisserial Opa proteins function as a family of adhesins that bind heparan sulfate proteoglycan (HSPG) or carcinoembryonic antigen family (CEACAM) receptors on human host cells. In order to define...

Identification of an outer membrane protein required for the transport of lipopolysaccharide to the bacterial cell surface

Bos, Martine P., Tefsen, Boris, Geurtsen, Jeroen, Tommassen, Jan

Lipopolysaccharide (LPS), also known as endotoxin due to its severe pathophysiological effects in infected subjects, is an essential component of the outer membrane (OM) of most Gram-negative...

Function of Neisserial Outer Membrane Phospholipase A in Autolysis and Assessment of Its Vaccine Potential

Bos, Martine P., Tefsen, Boris, Voet, Pierre, Weynants, Vincent, Van Putten, Jos P. M., Tommassen, Jan

Outer membrane phospholipase A (OMPLA) is an outer membrane-localized enzyme, present in many gram-negative bacterial species. It is implicated in the virulence of several pathogens. Here, we...

Viability of a Capsule- and Lipopolysaccharide-Deficient Mutant of Neisseria meningitidis

Bos, Martine P., Tommassen, Jan

Neisseria meningitidis is the only lipopolysaccharide (LPS)-producing gram-negative bacterial species shown to be viable also without LPS. It was thought that the presence of capsular polysaccharide...

Assembly Factor Omp85 Recognizes Its Outer Membrane Protein Substrates by a Species-Specific C-Terminal Motif

Robert, Viviane, Volokhina, Elena B, Senf, Freya, Bos, Martine P, Van Gelder, Patrick, Tommassen, Jan

Integral β-barrel proteins are found in the outer membranes of Gram-negative bacteria, mitochondria, and chloroplasts. The assembly of these proteins requires a proteinaceous apparatus of which...

CD66 receptor specificity exhibited by neisserial Opa variants is controlled by protein determinants in CD66 N-domains

Bos, Martine P., Kuroki, Motomu, Krop-Watorek, Anna, Hogan, Daniel, Belland, Robert J.

Neisseria gonorrhoeae strain MS11 is able to express 11 different opacity (Opa) proteins on its outer surface. A number of these Opa proteins have been shown to function as adhesins through binding...

Carcinoembryonic Antigen Family Receptor Recognition by Gonococcal Opa Proteins Requires Distinct Combinations of Hypervariable Opa Protein Domains

Bos, Martine P., Kao, David, Hogan, Daniel M., Grant, Christopher C. R., Belland, Robert J.

Neisserial Opa proteins function as a family of adhesins that bind heparan sulfate proteoglycan (HSPG) or carcinoembryonic antigen family (CEACAM) receptors on human host cells. In order to define...

Identification of an outer membrane protein required for the transport of lipopolysaccharide to the bacterial cell surface

Bos, Martine P., Tefsen, Boris, Geurtsen, Jeroen, Tommassen, Jan

Lipopolysaccharide (LPS), also known as endotoxin due to its severe pathophysiological effects in infected subjects, is an essential component of the outer membrane (OM) of most Gram-negative...

Function of Neisserial Outer Membrane Phospholipase A in Autolysis and Assessment of Its Vaccine Potential

Bos, Martine P., Tefsen, Boris, Voet, Pierre, Weynants, Vincent, Van Putten, Jos P. M., Tommassen, Jan

Outer membrane phospholipase A (OMPLA) is an outer membrane-localized enzyme, present in many gram-negative bacterial species. It is implicated in the virulence of several pathogens. Here, we...

Viability of a Capsule- and Lipopolysaccharide-Deficient Mutant of Neisseria meningitidis

Bos, Martine P., Tommassen, Jan

Neisseria meningitidis is the only lipopolysaccharide (LPS)-producing gram-negative bacterial species shown to be viable also without LPS. It was thought that the presence of capsular polysaccharide...

Assembly Factor Omp85 Recognizes Its Outer Membrane Protein Substrates by a Species-Specific C-Terminal Motif

Robert, Viviane, Volokhina, Elena B, Senf, Freya, Bos, Martine P, Van Gelder, Patrick, Tommassen, Jan

Integral β-barrel proteins are found in the outer membranes of Gram-negative bacteria, mitochondria, and chloroplasts. The assembly of these proteins requires a proteinaceous apparatus of which...

Additive and Synergistic Bactericidal Activity of Antibodies Directed against Minor Outer Membrane Proteins of Neisseria meningitidis▿

Weynants, Vincent E., Feron, Christiane M., Goraj, Karine K., Bos, Martine P., Denoël, Philippe A., Verlant, Vincent G., ...

Neisseria meningitidis serogroup B is a major cause of bacterial meningitis in younger populations. The available vaccines are based on outer membrane vesicles obtained from wild-type strains. In...

Homologue Scanning Mutagenesis Reveals Cd66 Receptor Residues Required for Neisserial Opa Protein Binding

Bos, Martine P., Hogan, Daniel, Belland, Robert J.

The immunoglobulin-like family of CD66 antigens, present on human neutrophils and epithelial cells, are used as receptors for adhesins expressed by the pathogenic Neisseriae. N. gonorrhoeae strain...

Functioning of outer membrane protein assembly factor Omp85 requires a single POTRA domain

Bos, Martine P, Robert, Viviane, Tommassen, Jan

β-Barrel proteins are present in the outer membranes of Gram-negative bacteria, mitochondria and chloroplasts. The central component of their assembly machinery is called Omp85 in bacteria. Omp85 is...

Signals in bacterial β-barrel proteins are functional in eukaryotic cells for targeting to and assembly in mitochondria

Walther, Dirk M., Papic, Drazen, Bos, Martine P., Tommassen, Jan, Rapaport, Doron

The outer membranes of Gram-negative bacteria, mitochondria, and chloroplasts harbor β-barrel proteins. The signals that allow precursors of such proteins to be targeted to mitochondria were not...