Sequence Diversity, Predicted Two-Dimensional Protein Structure, and Epitope Mapping of Neisserial Opa Proteins

Malorny, Burkhard; Morelli, Giovanna; Kušećek, Barica; Kolberg, Jan; Achtman, Mark

doi:10.1128/jb.180.5.1323-1330.1998

Cited by 95 publications

(69 citation statements)

References 50 publications

(79 reference statements)

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“…NspA displays high sequence homology with the neisserial Opa proteins, especially the membrane-spanning b -barrel domain. Based on this homology, Vandeputte-Rutten et al (2003) argue that it is likely that the fourth strand in the predicted topology model of Malorny et al . (1998) has to be shifted towards the extracellular side by eight residues (this recent finding was integrated in Figs 2, 5 and 6).…”

Section: Discussionmentioning

confidence: 99%

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Mapping the binding domains on meningococcal Opa proteins for CEACAM1 and CEA receptors

Jonge

Hamstra

Alphen

et al. 2003

Molecular Microbiology

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Section: Discussionmentioning

confidence: 99%

“…No binding to CEACAM3, 6 and 8 was observed. For Malorny et al ., 1998) of OpaA127, OpaB128, OpaD126 and OpaJ129. Identical amino acids within the hypervariable regions mutated in this study present in all four sequences are indicated in bold and underlined.…”

Section: The Four Opa Proteins Derived From H44/76 Are Invasion Assocmentioning

confidence: 99%

Mapping the binding domains on meningococcal Opa proteins for CEACAM1 and CEA receptors

Jonge

Hamstra

Alphen

et al. 2003

Molecular Microbiology

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“…The anti-Opa rabbit antiserum was produced by the following procedures: two peptides, STVSTDYFRNIRAHSI and HNWGRLENTRFKTHE, both of which correspond to the conserved amino acids of the outer face of the Opa protein (Malorny et al, 1998), were customized by Operon Biotechnologies (Japan). An antiserum specific for the oligopeptides was obtained by immunization of rabbits with the peptides coupled to keyhole limpet hemocyanin using m-maleimidobenzoyl-N-hydroxysuccinimide ester (MBS).…”

Section: Production Of Anti-pilc Rabbit Antiserum and Anti-opa Rabbitmentioning

confidence: 99%

Differentialin vitroinfectious abilities of two common Japan-specific sequence-type (ST) clones of disease-associated ST-2032 and carrier-associated ST-2046Neisseria meningitidis strainsin human endothelial and epithelial cell lines

Takahashi

Kim

Watanabe

2008

FEMS Immunol Med Microbiol

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The Japan-specific sequence type (ST) clones, as well as several major epidemic-prone clones such as ST-32, have been identified previously among Neisseria meningitidis isolates in Japan. In this study, the infectious properties of various ST clones, including the two common Japan-specific ones, were examined and compared by in vitro infection assays using human endothelial and epithelial cell lines. The known invasive clones, as well as the Japan-specific ST-2032 strains that were frequently isolated from patients, exhibited high infectious abilities in adherence and invasion. In contrast, the Japan-specific ST-2046 and ST-198 strains, both of which were frequently isolated from carriers in Japan, were less efficient in adherence and invasion. The expression of the bacterial surface molecules such as pilin, Opc, Opa and PilC, and the lipooligosaccharide structure, did not differ between disease-associated and carrier-associated isolates. These results suggest that in vitro infection assays may discriminate between disease-associated (patient-dominant) and carrier-associated (carrier-dominant) meningococcal ST clones. The ST-2032 clone showed the highest infectious activity in vitro, suggesting that it may possess some unidentified factors necessary for the infectious ability that were not present in the ST-2046 clone with the lowest infectious ability.

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“…If necessary, alignments were edited manually by placing gaps such that they increased DNA sequence similarities. The percentage uniformity, defined as the percentage of the most frequent nucleotide at each position (excluding gaps introduced by the alignment), was determined with the program PsFind (Malorny et al, 1998). The percentage diversity is 100 minus the percentage uniformity.…”

Section: Dna Sequence Analysismentioning

confidence: 99%

Genesis of BRO β‐lactamase‐producing Moraxella catarrhalis: evidence for transformation‐mediated horizontal transfer

Bootsma

Dijk²,

Vauterin³

et al. 2000

Molecular Microbiology

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SummaryThe dramatic rise in BRO-producing M. catarrhalis strains observed in the last decades is without precedence. The aim of this study was to elucidate the events that led to the emergence of BRO-1 and BRO-2 b-lactamases. Previously, we showed bro1 and bro2 to be .99% identical. Data presented here suggested that bro2 was acquired by a fortuitous event and inserted between M. catarrhalis genes orf1 and orf3. Subsequently, bro1 evolved from bro2. Promoter-up mutations increased fitness of bro2, explaining its present predominance. The highly conserved nature of bro compared with orf1 and orf3 suggested that acquisition has occurred relatively recently. The random distribution of bro among M. catarrhalis fingerprint types indicated that bro has spread by horizontal transfer. Sequence analysis revealed that 80±200 bp is generally cotransferred with bro, serving as regions of homology that target bro to the same chromosomal locus. A region of 160 bases upstream of bro1 lacked polymorphism, indicating it was derived from the original strain that acquired bro2. We observed that bro was readily transferred by transformation between M. catarrhalis strains in vitro, suggesting a mechanism by which bro has disseminated. In conclusion, we have been able to reconstruct the steps that led to the emergence of BRO-producing M. catarrhalis.

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Sequence Diversity, Predicted Two-Dimensional Protein Structure, and Epitope Mapping of Neisserial Opa Proteins

Cited by 95 publications

References 50 publications

Mapping the binding domains on meningococcal Opa proteins for CEACAM1 and CEA receptors

Mapping the binding domains on meningococcal Opa proteins for CEACAM1 and CEA receptors

Differentialin vitroinfectious abilities of two common Japan-specific sequence-type (ST) clones of disease-associated ST-2032 and carrier-associated ST-2046Neisseria meningitidis strainsin human endothelial and epithelial cell lines

Genesis of BRO β‐lactamase‐producing Moraxella catarrhalis: evidence for transformation‐mediated horizontal transfer

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