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Book: Neisseria meningitidis

Seib, Kate L. / Peak, Ian R.

methods and protocols

(Methods in molecular biology ; 1969 ; Springer protocols)

2019

Author's details	edited by Kate L. Seib and Ian R. Peak
Series title	Methods in molecular biology ; 1969 Springer protocols
Collection
Language	English
Size	xiii, 253 Seiten, Illustrationen
Publisher	Humana Press
Publishing place	New York, NY
Publishing country	United States
Document type	Book
HBZ-ID	HT020011874
ISBN	978-1-4939-9201-0 ; 9781493992027 ; 1-4939-9201-5 ; 1493992023
Database	Catalogue ZB MED Medicine, Health

In stock of ZB MED Cologne/Königswinter

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Zs A 7042 -1969-	verfügbar in Königswinter	Königswinter

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Article: Otitis media: recent advances in otitis media vaccine development and model systems.

Zahid, Ayesha / Wilson, Jennifer C / Grice, I Darren / Peak, Ian R

Frontiers in microbiology

2024 Volume 15, Page(s) 1345027

Abstract: Otitis media is an inflammatory disorder of the middle ear caused by airways-associated bacterial or viral infections. It is one of the most common childhood infections as globally more than 80% of children are diagnosed with acute otitis media by 3 ... ...

Abstract	Otitis media is an inflammatory disorder of the middle ear caused by airways-associated bacterial or viral infections. It is one of the most common childhood infections as globally more than 80% of children are diagnosed with acute otitis media by 3 years of age and it is a common reason for doctor's visits, antibiotics prescriptions, and surgery among children. Otitis media is a multifactorial disease with various genetic, immunologic, infectious, and environmental factors predisposing children to develop ear infections.
Language	English
Publishing date	2024-01-24
Publishing country	Switzerland
Document type	Journal Article ; Review
ZDB-ID	2587354-4
ISSN	1664-302X
ISSN	1664-302X
DOI	10.3389/fmicb.2024.1345027
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Article ; Online: Characterisation of a capsular polysaccharide from Moraxella nonliquefaciens CCUG 348T.

Ravikumaran, Kosala S / Armiento, Samantha / De Castro, Cristina / Molinaro, Antonio / Wilson, Jennifer C / Grice, I Darren / Peak, Ian R

Carbohydrate research

2024 Volume 538, Page(s) 109095

Abstract: Moraxella nonliquefaciens is a commensal of the human upper respiratory tract (URT) but on rare occasions is recovered in cases of ocular, septic and pulmonary infections. Hence there is interest in the pathogenic determinants of M. nonliquefaciens, of ... ...

Abstract	Moraxella nonliquefaciens is a commensal of the human upper respiratory tract (URT) but on rare occasions is recovered in cases of ocular, septic and pulmonary infections. Hence there is interest in the pathogenic determinants of M. nonliquefaciens, of which outer membrane (OM) structures such as fimbriae and two capsular polysaccharide (CPS) structures, →3)-β-D-GalpNAc-(1→5)-β-Kdop-(2→ and →8)-α-NeuAc-(2→, have been reported in the literature. To further characterise its surface virulence factors, we isolated a novel CPS from M. nonliquefaciens type strain CCUG 348T. This structure was elucidated using NMR data obtained from CPS samples that were subjected to various degrees of mild acid hydrolysis. Together with GLC-MS data, the structure was resolved as a linear polymer composed of two GalfNAc residues consecutively added to Kdo, →3)-β-D-GalfNAc-(1→3)-α-D-GalfNAc-(1→5)-α-(8-OAc)Kdop-(2→. Supporting evidence for this material being CPS was drawn from the proposed CPS biosynthetic locus which encoded a potential GalfNAc transferase, a UDP-GalpNAc mutase for UDP-GalfNAc production and a putative CPS polymerase with predicted GalfNAc and Kdo transferase domains. This study describes a unique CPS composition reported in Moraxella spp. and offers genetic insights into the synthesis and expression of GalfNAc residues, which are rare in bacterial OM glycans.
MeSH term(s)	Humans ; Polysaccharides/analysis ; Moraxella ; Transferases/analysis ; Uridine Diphosphate/analysis ; Bacterial Capsules/chemistry ; Polysaccharides, Bacterial/chemistry
Chemical Substances	Polysaccharides ; Transferases (EC 2.-) ; Uridine Diphosphate (58-98-0) ; Polysaccharides, Bacterial
Language	English
Publishing date	2024-03-15
Publishing country	Netherlands
Document type	Journal Article
ZDB-ID	1435-7
ISSN	1873-426X ; 0008-6215
ISSN (online)	1873-426X
ISSN	0008-6215
DOI	10.1016/j.carres.2024.109095
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Article ; Online: Moraxella ovis and Moraxella bovoculi lipooligosaccharide biosynthesis genes, and structural characterisation of oligosaccharide from M. ovis 354T.

Ravikumaran, Kosala S / King, Rebecca M / Notaro, Anna / Molinaro, Antonio / de Castro, Cristina / Wilson, Jennifer C / Grice, I Darren / Peak, Ian R

Carbohydrate research

2024 Volume 536, Page(s) 109043

Abstract: Moraxella ovis is a Gram-negative bacterium isolated from sheep conjunctivitis cases and is a rare isolate of infectious bovine keratoconjunctivitis (IBK). This species is closely related to M. bovoculi, another species which can also be isolated from ... ...

Abstract	Moraxella ovis is a Gram-negative bacterium isolated from sheep conjunctivitis cases and is a rare isolate of infectious bovine keratoconjunctivitis (IBK). This species is closely related to M. bovoculi, another species which can also be isolated from IBK, or cattle upper respiratory tract (URT). Prior to molecular identification techniques, M. bovoculi was frequently misclassified as M. ovis. We previously described the structure of two oligosaccharides (lipooligosaccharide-derived, minor and major glycoforms) from M. bovoculi 237T (type strain, also ATCC BAA-1259T). Here, we have identified the genetic loci for lipooligosaccharide synthesis in M. ovis 354T (NCTC11227) and compared it with M. bovoculi 237T. We identified genes encoding the known glycosyltransferases Lgt6 and Lgt3 in M.ovis. These genes are conserved in Moraxella spp., including M bovoculi. We identified three further putative OS biosynthesis genes that are restricted to M. ovis and M. bovoculi. These encode enzymes predicted to function as GDP-mannose synthases, namely a mannosyltransferase and a glycosyltransferase. Adding insight into the genetic relatedness of M.ovis and M. bovoculi, the M. ovis genes have higher similarity to those in M. bovoculi genotype 2 (nasopharyngeal isolates from asymptomatic cattle), than to M. bovoculi genotype 1 (isolates from eyes of IBK-affected cattle). Sequence analysis confirmed that the predicted mannosyltransferase in M. bovoculi 237T is interrupted by a C>T polymorphism. This mutation is not present in other M. bovoculi strains sequenced to date. We isolated and characterised LOS-derived oligosaccharide from M. ovis 354T. GLC-MS and NMR spectroscopy data revealed a heptasaccharide structure with three β-D-Glcp residues attached as branches to the central 3,4,6-α-D-Glcp, with subsequent attachment to Kdo. This inner core arrangement is consistent with the action of Lgt6 and Lgt3 glycosyltransferases. Two α-D-Manp residues are linearly attached to the 4-linked β-D-Glcp, consistent with the presence of the two identified glycosyltransferases. This oligosaccharide structure is consistent with the previously reported minor glycoform isolated from M. bovoculi 237T.
MeSH term(s)	Animals ; Cattle ; Sheep ; Mannosyltransferases ; Keratoconjunctivitis, Infectious/microbiology ; Moraxella/genetics ; Glycosyltransferases/genetics ; Oligosaccharides ; Lipopolysaccharides
Chemical Substances	lipid-linked oligosaccharides ; Mannosyltransferases (EC 2.4.1.-) ; Glycosyltransferases (EC 2.4.-) ; Oligosaccharides ; Lipopolysaccharides
Language	English
Publishing date	2024-01-24
Publishing country	Netherlands
Document type	Journal Article
ZDB-ID	1435-7
ISSN	1873-426X ; 0008-6215
ISSN (online)	1873-426X
ISSN	0008-6215
DOI	10.1016/j.carres.2024.109043
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Article ; Online: Proteome of a Moraxella catarrhalis Strain under Iron-Restricted Conditions.

Blakeway, Luke V / Tan, Aimee / Peak, Ian R / Atack, John M / Seib, Kate L

Microbiology resource announcements

2020 Volume 9, Issue 12

Abstract: Moraxella ... ...

Abstract	Moraxella catarrhalis
Language	English
Publishing date	2020-03-19
Publishing country	United States
Document type	Journal Article
ISSN	2576-098X
ISSN (online)	2576-098X
DOI	10.1128/MRA.00064-20
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Article ; Online: Transcriptome RNA Sequencing Data Set of Gene Expression in Moraxella catarrhalis On- and Off-Phase Variants of the Type III DNA Methyltransferase ModM3.

Blakeway, Luke V / Tan, Aimee / Peak, Ian R / Atack, John M / Seib, Kate L

Microbiology resource announcements

2020 Volume 9, Issue 14

Abstract: Moraxella ... ...

Abstract	Moraxella catarrhalis
Language	English
Publishing date	2020-04-02
Publishing country	United States
Document type	Journal Article
ISSN	2576-098X
ISSN (online)	2576-098X
DOI	10.1128/MRA.01559-19
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Article: Immunological characterisation of truncated lipooligosaccharide-outer membrane protein based conjugate vaccine against Moraxella catarrhalis and nontypeable Haemophilus influenzae

Singh, Sanjesh / Cripps, Allan W / Grice, I. Darren / Massa, Helen / Ozberk, Victoria / Peak, Ian R / Wilson, Jennifer C

Vaccine. 2020 Jan. 10, v. 38, no. 2

2020

Abstract: Moraxella catarrhalis and nontypeable Haemophilus influenzae are important bacterial causes of otitis media in children and respiratory diseases in adults. Lipooligosaccharide (LOS) from M. catarrhalis and outer membrane protein 26 (OMP26) from NTHi are ... ...

Abstract	Moraxella catarrhalis and nontypeable Haemophilus influenzae are important bacterial causes of otitis media in children and respiratory diseases in adults. Lipooligosaccharide (LOS) from M. catarrhalis and outer membrane protein 26 (OMP26) from NTHi are major surface antigens identified as potential vaccine components against these organisms. We previously constructed M. catarrhalis in which LOS is truncated, but contains a structure common to the three known serotypes of M. catarrhalis. OMP26 is known to enhance clearance of NTHi following vaccination in animal models, so was chosen as the carrier protein. In this study, we conjugated wild-type and truncated M. catarrhalis detoxified-LOS to a recombinant modified OMP26, rOMP26VTAL. Vaccination of mice with these conjugates resulted in a significant increase in anti-LOS and anti-rOMP26VTAL IgG levels. Importantly, mouse antisera showed complement-mediated bactericidal activity against all M. catarrhalis serotype A and B strains and a NTHi strain tested. Serotypes A & B make up more than 90% of isolates. These data suggest that the LOS and OMP based conjugate can be used as vaccine components and require further investigation in animal models.
Keywords	adults ; animal models ; antibacterial properties ; antiserum ; children ; complement ; Haemophilus influenzae ; immunoglobulin G ; lipooligosaccharides ; mice ; Moraxella catarrhalis ; otitis media ; outer membrane proteins ; respiratory tract diseases ; serotypes ; surface antigens ; vaccination ; vaccines
Language	English
Dates of publication	2020-0110
Size	p. 309-317.
Publishing place	Elsevier Ltd
Document type	Article
ZDB-ID	605674-x
ISSN	1873-2518 ; 0264-410X
ISSN (online)	1873-2518
ISSN	0264-410X
DOI	10.1016/j.vaccine.2019.10.014
Database	NAL-Catalogue (AGRICOLA)

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Article: Structural characterisation of the oligosaccharide from Moraxella bovoculi type strain 237 (ATCC BAA-1259) lipooligosaccharide

Grice, I. Darren / Peak, Ian R / Dawood, Wisam A / King, Rebecca M / Ravikumaran, Kosala S / Speciale, Immacolata / Molinaro, Antonio / de Castro, Cristina / Wilson, Jennifer C

Carbohydrate research. 2021 May, v. 503

2021

Abstract: The Gram-negative bacterium Moraxella bovoculi is associated with infectious bovine keratoconjunctivitis (IBK), colloquially known as ‘pink-eye’. IBK is an extremely contagious ocular disease of cattle. We report here the structure of the oligosaccharide ...

Abstract	The Gram-negative bacterium Moraxella bovoculi is associated with infectious bovine keratoconjunctivitis (IBK), colloquially known as ‘pink-eye’. IBK is an extremely contagious ocular disease of cattle. We report here the structure of the oligosaccharide derived from the lipooligosaccharide from M. bovoculi type strain 237 (also known as ATCC BAA-1259T). GLC-MS and correlation NMR analysis of the oligosaccharide revealed 5 sugar residues, with a notable central branched 3,4,6-α-D-Glcp. An additional α-D-Manp was present ~30% on the sub-terminal α-D-Manp of the 4-linked branch. This oligosaccharide structure was consistent with other members of the Moraxellaceae where no heptose was present and 5-linked Kdo was directly attached to the central 3,4,6-α-D-Glcp.
Keywords	Gram-negative bacteria ; Moraxella bovoculi ; cattle ; keratoconjunctivitis ; lipooligosaccharides ; research
Language	English
Dates of publication	2021-05
Publishing place	Elsevier Ltd
Document type	Article
Note	NAL-AP-2-clean
ZDB-ID	1435-7
ISSN	1873-426X ; 0008-6215
ISSN (online)	1873-426X
ISSN	0008-6215
DOI	10.1016/j.carres.2021.108293
Database	NAL-Catalogue (AGRICOLA)

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Article ; Online: Virulence determinants of Moraxella catarrhalis: distribution and considerations for vaccine development.

Blakeway, Luke V / Tan, Aimee / Peak, Ian R A / Seib, Kate L

Microbiology (Reading, England)

2017 Volume 163, Issue 10, Page(s) 1371–1384

Abstract: Moraxella catarrhalis is a human-restricted opportunistic bacterial pathogen of the respiratory mucosa. It frequently colonizes the nasopharynx asymptomatically, but is also an important causative agent of otitis media (OM) in children, and plays a ... ...

Abstract	Moraxella catarrhalis is a human-restricted opportunistic bacterial pathogen of the respiratory mucosa. It frequently colonizes the nasopharynx asymptomatically, but is also an important causative agent of otitis media (OM) in children, and plays a significant role in acute exacerbations of chronic obstructive pulmonary disease (COPD) in adults. As the current treatment options for M. catarrhalis infection in OM and exacerbations of COPD are often ineffective, the development of an efficacious vaccine is warranted. However, no vaccine candidates for M. catarrhalis have progressed to clinical trials, and information regarding the distribution of M. catarrhalis virulence factors and vaccine candidates is inconsistent in the literature. It is largely unknown if virulence is associated with particular strains or subpopulations of M. catarrhalis, or if differences in clinical manifestation can be attributed to the heterogeneous expression of specific M. catarrhalis virulence factors in the circulating population. Further investigation of the distribution of M. catarrhalis virulence factors in the context of carriage and disease is required so that vaccine development may be targeted at relevant antigens that are conserved among disease-causing strains. The challenge of determining which of the proposed M. catarrhalis virulence factors are relevant to human disease is amplified by the lack of a standardized M. catarrhalis typing system to facilitate direct comparisons of worldwide isolates. Here we summarize and evaluate proposed relationships between M. catarrhalis subpopulations and specific virulence factors in the context of colonization and disease, as well as the current methods used to infer these associations.
MeSH term(s)	Animals ; Bacterial Proteins/genetics ; Bacterial Proteins/immunology ; Bacterial Vaccines/immunology ; Humans ; Moraxella catarrhalis/classification ; Moraxella catarrhalis/genetics ; Moraxella catarrhalis/immunology ; Moraxella catarrhalis/pathogenicity ; Moraxellaceae Infections/drug therapy ; Moraxellaceae Infections/immunology ; Moraxellaceae Infections/microbiology ; Moraxellaceae Infections/prevention & control ; Otitis Media/drug therapy ; Otitis Media/immunology ; Otitis Media/microbiology ; Otitis Media/prevention & control ; Pulmonary Disease, Chronic Obstructive/drug therapy ; Pulmonary Disease, Chronic Obstructive/immunology ; Pulmonary Disease, Chronic Obstructive/microbiology ; Pulmonary Disease, Chronic Obstructive/prevention & control ; Virulence/genetics ; Virulence/immunology ; Virulence Factors/genetics ; Virulence Factors/immunology
Chemical Substances	Bacterial Proteins ; Bacterial Vaccines ; Virulence Factors
Language	English
Publishing date	2017-09-12
Publishing country	England
Document type	Journal Article ; Review
ZDB-ID	1180712-x
ISSN	1465-2080 ; 1350-0872
ISSN (online)	1465-2080
ISSN	1350-0872
DOI	10.1099/mic.0.000523
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Article ; Online: Moraxella catarrhalis phase-variable loci show differences in expression during conditions relevant to disease.

Tan, Aimee / Blakeway, Luke V / Taha / Yang, Yuedong / Zhou, Yaoqi / Atack, John M / Peak, Ian R / Seib, Kate L

PloS one

2020 Volume 15, Issue 6, Page(s) e0234306

Abstract: Moraxella catarrhalis is a human-adapted, opportunistic bacterial pathogen of the respiratory mucosa. Although asymptomatic colonization of the nasopharynx is common, M. catarrhalis can ascend into the middle ear, where it is a prevalent causative agent ... ...

Abstract	Moraxella catarrhalis is a human-adapted, opportunistic bacterial pathogen of the respiratory mucosa. Although asymptomatic colonization of the nasopharynx is common, M. catarrhalis can ascend into the middle ear, where it is a prevalent causative agent of otitis media in children, or enter the lower respiratory tract, where it is associated with acute exacerbations of chronic obstructive pulmonary disease in adults. Phase variation is the high frequency, random, reversible switching of gene expression that allows bacteria to adapt to different host microenvironments and evade host defences, and is most commonly mediated by simple DNA sequence repeats. Bioinformatic analysis of five closed M. catarrhalis genomes identified 17 unique simple DNA sequence repeat tracts that were variable between strains, indicating the potential to mediate phase variable expression of the associated genes. Assays designed to assess simple sequence repeat variation under conditions mimicking host infection demonstrated that phase variation of uspA1 (ubiquitous surface protein A1) from high to low expression occurs over 72 hours of biofilm passage, while phase variation of uspA2 (ubiquitous surface protein A2) to high expression variants occurs during repeated exposure to human serum, as measured by mRNA levels. We also identify and confirm the variable expression of two novel phase variable genes encoding a Type III DNA methyltransferase (modO), and a conserved hypothetical permease (MC25239_RS00020). These data reveal the repertoire of phase variable genes mediated by simple sequence repeats in M. catarrhalis and demonstrate that modulation of expression under conditions mimicking human infection is attributed to changes in simple sequence repeat length.
MeSH term(s)	Bacterial Adhesion/genetics ; Bacterial Outer Membrane Proteins/genetics ; Bacterial Outer Membrane Proteins/metabolism ; Gene Expression/genetics ; Gene Expression Regulation, Bacterial/genetics ; Humans ; Microsatellite Repeats/genetics ; Moraxella catarrhalis/genetics ; Moraxella catarrhalis/pathogenicity ; Moraxellaceae Infections ; Otitis Media/microbiology ; Repetitive Sequences, Nucleic Acid/genetics
Chemical Substances	Bacterial Outer Membrane Proteins ; UspA protein, Moraxella catarrhalis
Language	English
Publishing date	2020-06-18
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ISSN	1932-6203
ISSN (online)	1932-6203
DOI	10.1371/journal.pone.0234306
Database	MEDical Literature Analysis and Retrieval System OnLINE

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