Distribution of specific DNA sequences among pathogenic and commensal Neisseria species

Aho, Ellen L.; Murphy, George L.; Cannon, Janne G.

doi:10.1128/iai.55.4.1009-1013.1987

Cited by 55 publications

(22 citation statements)

References 32 publications

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“…The pilS and pilE probes did not hybridize with commensal Neisseria species (a possible exception was a weak signal seen with pits and N. subflava). a finding noted previously (Aho and Cannon, 1987). Thus, in commensal strains, FKBP genes were not linked to known pilin loci.…”

Section: Location Of Fkbp-like Genes In the Meningococcal And Commenssupporting

confidence: 70%

Analysis in Neisseria meningitidis and other Neisseria species of genes homologous to the FKBP immunophilin family

McAllister

Stephens

1993

Molecular Microbiology

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The immunophilin family of FK506-binding proteins (FKBPs), involved in eukaryotic protein-folding and cell regulation, have recently been found to have prokaryotic homologues. Genes with sequences homologous to those encoding human FKBPs were examined in Neisseria species. An FKBP DNA sequence was present, as shown by the polymerase chain reaction and Southern blotting experiments, in the chromosome of Neisseria meningitidis (14 strains) and in all 11 different commensal Neisseria spp. studied, but was not found in Neisseria gonorrhoeae (11 strains tested) or in Moraxella catarrhalis. The nucleotide and predicted protein sequences of the FKBP-encoding domain from five of the meningococcal strains were highly conserved (e.g. > or = 97% homologous). The meningococcal nucleotide sequence was > or = 93% homologous and the consensus meningococcal protein sequence was > or = 97% homologous to FKBP sequences found in seven different commensal Neisseria spp. The meningococcal nucleotide and predicted protein sequences were > or = 59% homologous to the conserved C-terminus of the human FKBP gene family. The FKBP nucleotide sequence was present as a single copy in the chromosome of commensal Neisseria spp. and in most strains of N. meningitidis. The FKBP gene was linked to the silent pilin locus, pilS, in class II-piliated meningococcal strains. In meningococcal strains expressing class I pili, the FKBP gene was linked to one of several pilS loci but not the pilE locus present in these strains. FKBP genes found in commensal Neisseria spp. were not linked to known pilin loci.

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Section: Location Of Fkbp-like Genes In the Meningococcal And Commenssupporting

confidence: 70%

Analysis in Neisseria meningitidis and other Neisseria species of genes homologous to the FKBP immunophilin family

McAllister

Stephens

1993

Molecular Microbiology

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“…Western blotting of whole cell lysates of commensal strains using the mAb B33 raised against pathogenic Opa protein demonstrated the expression of Opa proteins by all of the Cn tested. In earlier studies, the presence of opa genes in various commensal isolates was observed, but their expression was not detected (Aho et al, 1987;Wolff and Stern, 1995).…”

Section: Discussionmentioning

confidence: 88%

“…To date, studies on Cn have indicated that, in general, they have a limited repertoire of pathogenic determinants. Studies on 12 commensal neisserial strains failed to detect opc-like genes (Zhu et al, 1999), whereas pilin genes have been detected in several human commensal neisserial isolates tested (Aho et al, 1987). Commensal genes homologous to pathogenic neisserial opa have been identified in previous studies, but their expression was not detected (Wolff and Stern, 1995).…”

Section: Introductionmentioning

confidence: 98%

Expression of pathogen-like Opa adhesins in commensal Neisseria: genetic and functional analysis

2001

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Several species of commensal Neisseriae (Cn) may colonize the human nasopharynx, but little is known about their adhesion mechanisms. We have investigated structural and functional similarities between adhesins of Cn and of Neisseria meningitidis (Nm), also a frequent colonizer of the nasopharynx. In this study, we demonstrate the expression of Opa‐like proteins in nine strains of Cn. Phylogenetic analysis segregated the majority of the Cn Opa in a cluster separated from the pathogenic cluster with a few exceptions. One Opa, which located within the pathogenic cluster, was strikingly similar (74%) to an Opa of a Neisseria gonorrhoeae (Ng) strain and, like Ng, it lacked the extra Y11 or the 136DKF138 triplet insert, which are conserved among many N. meningitidis Opa proteins. Most importantly, the majority of the Cn Opa proteins were able to interact with human CEACAM1 (CD66a) molecules, previously identified as receptors for pathogenic Opa proteins. By the use of CEACAM1 N‐domain mutants, we demonstrate that Cn Opa target the same region of the N‐domain of the receptor as that used by Nm. Furthermore, Cn strains bound to cell‐expressed human CEACAM1. In competition assays, adherent Cn strain C450, exhibiting high affinity for CEACAM1, was not displaced by a Nm isolate and vice versa. But in simultaneous incubation, Nm out‐competed the Cn strain. This is the first study to demonstrate the expression of adhesins in Cn that are structurally and functionally closely related to pathogenic adhesins. The studies imply that some Cn have the potential to occupy and thus compete with the pathogens for receptors on human mucosa, their common and exclusive niche.

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“…However, more detailed investigations imply that some of these factors are more widely distributed. Pili, a well known virulence factor in gonococcal and meningococcal infection, have also been observed on commensal Neisseria species [2]. The opacity protein (Opal, an outer membrane protein of gonococci, seem to have an equivalent in meningococci, formerly designated as class 5 proteins.…”

Section: Introductionmentioning

confidence: 99%

Identification and characterization of specific sequences encoding pathogenicity associated proteins in the genome of commensal Neisseria species

Wolff

1995

FEMS Microbiology Letters

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The distribution of distinct sequences in pathogenic and commensal Neisseria species was investigated systematically by dot blot analysis. Probes representing the genes of Rmp, pilin and IgA1 protease were found to hybridize exclusively to the chromosomal DNA of the pathogenic species, Neisseria gonorrhoeae and/or Neisseria meningitidis. In contrast, specific sequences for the genes of the porin protein Por and the opacity protein (Opa) were also detected in a panel of commensal Neisseria species such as N. lactamica, N. subflava, N. flava, N. mucosa and N. sicca. Using opa-specific oligonucleotides as probes in chromosomal blots, the genomes of the commensal Neisseria species show a totally reduced repertoire of cross-hybridizing loci compared to the complex opa gene family of N. gonorrhoeae. DNA sequence analysis of one opa-related gene derived from N. flava and N. sicca, respectively, revealed a large degree of homology with previously described gonococcal and meningococcal genes, e.g., a typical repetitive sequence in the leader peptide and the distribution of the hypervariable and conserved regions. This observation, together with the finding, that the gene is constitutively transcribed, leads to the assumption that some of the commensal Neisseria species may have the potential for the expression of a protein harboring similar functions as the Opa proteins in pathogenic Neisseriae.

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Distribution of specific DNA sequences among pathogenic and commensal Neisseria species

Cited by 55 publications

References 32 publications

Analysis in Neisseria meningitidis and other Neisseria species of genes homologous to the FKBP immunophilin family

Analysis in Neisseria meningitidis and other Neisseria species of genes homologous to the FKBP immunophilin family

Expression of pathogen-like Opa adhesins in commensal Neisseria: genetic and functional analysis

Identification and characterization of specific sequences encoding pathogenicity associated proteins in the genome of commensal Neisseria species

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