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A role for fibroblast growth factor receptor 1 in the pathogenesis of Neisseria meningitidis (2020)
Journal Article
Azimi, S., Wheldon, L. M., Oldfield, N. J., Ala'Aldeen, D. A., & Wooldridge, K. G. (2020). A role for fibroblast growth factor receptor 1 in the pathogenesis of Neisseria meningitidis. Microbial Pathogenesis, 149, Article 104534. https://doi.org/10.1016/j.micpath.2020.104534

Neisseria meningitidis (the meningococcus) remains an important cause of human disease, including meningitis and sepsis. Adaptation to the host environment includes many interactions with specific cell surface receptors, resulting in intracellular si... Read More about A role for fibroblast growth factor receptor 1 in the pathogenesis of Neisseria meningitidis.

Variant Signal Peptides of Vaccine Antigen, FHbp, Impair Processing Affecting Surface Localization and Antibody-Mediated Killing in Most Meningococcal Isolates (2019)
Journal Article
da Silva, R. A., Karlyshev, A. V., Oldfield, N. J., Wooldridge, K. G., Bayliss, C. D., Ryan, A., & Griffin, R. (2019). Variant Signal Peptides of Vaccine Antigen, FHbp, Impair Processing Affecting Surface Localization and Antibody-Mediated Killing in Most Meningococcal Isolates. Frontiers in Microbiology, 10, Article 2847. https://doi.org/10.3389/fmicb.2019.02847

© Copyright © 2019 da Silva, Karlyshev, Oldfield, Wooldridge, Bayliss, Ryan and Griffin. Meningococcal lipoprotein, Factor H binding protein (FHbp), is the sole antigen of the Trumenba vaccine (Pfizer) and one of four antigens of the Bexsero vaccine... Read More about Variant Signal Peptides of Vaccine Antigen, FHbp, Impair Processing Affecting Surface Localization and Antibody-Mediated Killing in Most Meningococcal Isolates.

The moonlighting peroxiredoxin-glutaredoxin in Neisseria meningitidis binds plasminogen via a C-terminal lysine residue and contributes to survival in a whole blood model (2019)
Journal Article
Aljannat, M. A., Oldfield, N. J., Albasri, H. M., Dorrington, L. K., Ohri, R. L., Wooldridge, K. G., & Turner, D. P. (2020). The moonlighting peroxiredoxin-glutaredoxin in Neisseria meningitidis binds plasminogen via a C-terminal lysine residue and contributes to survival in a whole blood model. Microbial Pathogenesis, 139, Article 103890. https://doi.org/10.1016/j.micpath.2019.103890

© 2019 Elsevier Ltd Neisseria meningitidis is a human-restricted bacterium that can invade the bloodstream and cross the blood-brain barrier resulting in life-threatening sepsis and meningitis. Meningococci express a cytoplasmic peroxiredoxin-glutare... Read More about The moonlighting peroxiredoxin-glutaredoxin in Neisseria meningitidis binds plasminogen via a C-terminal lysine residue and contributes to survival in a whole blood model.

Moonlighting Functions of Bacterial Fructose 1,6-Bisphosphate Aldolases (2017)
Book Chapter
Oldfield, N. J., Shams, F., Wooldridge, K. G., & Turner, D. P. (2017). Moonlighting Functions of Bacterial Fructose 1,6-Bisphosphate Aldolases. In B. Henderson (Ed.), Moonlighting Proteins: Novel Virulence Factors in Bacterial Infections (321-331). Wiley

© 2017 John Wiley & Sons, Inc. Moonlighting proteins are multifunctional proteins which perform two or more biochemical functions using a single polypeptide chain. Moonlighting proteins have been documented in diverse organisms, including archaea,... Read More about Moonlighting Functions of Bacterial Fructose 1,6-Bisphosphate Aldolases.

Fructose-1,6-bisphosphate aldolase of Neisseria meningitidis binds human plasminogen via its C-terminal lysine residue (2016)
Journal Article
Shams, F., Oldfield, N. J., Lai, S. K., Tunio, S. A., Wooldridge, K. G., & Turner, D. P. (2016). Fructose-1,6-bisphosphate aldolase of Neisseria meningitidis binds human plasminogen via its C-terminal lysine residue. Microbiology Open, 5(2), https://doi.org/10.1002/mbo3.331

Neisseria meningitidis is a leading cause of fatal sepsis and meningitis worldwide. As for commensal species of human neisseriae, N. meningitidis inhabits the human nasopharynx and asymptomatic colonization is ubiquitous. Only rarely does the organis... Read More about Fructose-1,6-bisphosphate aldolase of Neisseria meningitidis binds human plasminogen via its C-terminal lysine residue.

Fructose-1,6-bisphosphate aldolase (FBA)-A conserved glycolytic enzyme with virulence functions in bacteria: 'Ill met by moonlight' (2014)
Journal Article
Shams, F., Oldfield, N. J., Wooldridge, K. G., & Turner, D. P. J. (2014). Fructose-1,6-bisphosphate aldolase (FBA)-A conserved glycolytic enzyme with virulence functions in bacteria: 'Ill met by moonlight'. Biochemical Society Transactions, 42(6), 1792-1795. https://doi.org/10.1042/BST20140203

© 2014 Biochemical Society. Moonlighting proteins constitute an intriguing class of multifunctional proteins. Metabolic enzymes and chaperones, which are often highly conserved proteins in bacteria, archaea and eukaryotic organisms, are among the mos... Read More about Fructose-1,6-bisphosphate aldolase (FBA)-A conserved glycolytic enzyme with virulence functions in bacteria: 'Ill met by moonlight'.

A novel O-linked glycan modulates Campylobacter jejuni major outer membrane protein-mediated adhesion to human histo-blood group antigens and chicken colonization (2014)
Journal Article
Mahdavi, J., Pirinccioglu, N., Oldfield, N. J., Carlsohn, E., Stoof, J., Aslam, A., …Ala'Aldeen, D. A. (2014). A novel O-linked glycan modulates Campylobacter jejuni major outer membrane protein-mediated adhesion to human histo-blood group antigens and chicken colonization. Open Biology, 4(1), Article 130202. https://doi.org/10.1098/rsob.130202

Campylobacter jejuni is an important cause of human foodborne gastroenteritis; strategies to prevent infection are hampered by a poor understanding of the complex interactions between host and pathogen. Previous work showed that C. jejuni could bind... Read More about A novel O-linked glycan modulates Campylobacter jejuni major outer membrane protein-mediated adhesion to human histo-blood group antigens and chicken colonization.

Mapping the laminin receptor binding domains of Neisseria meningitidis PorA and Haemophilus influenzae OmpP2 (2012)
Journal Article
Abouseada, N. M., Assafi, M. S. A., Mahdavi, J., Oldfield, N. J., Wheldon, L. M., Wooldridge, K. G., & Ala'Aldeen, D. A. (2012). Mapping the laminin receptor binding domains of Neisseria meningitidis PorA and Haemophilus influenzae OmpP2. PLoS ONE, 7(9), Article 10. https://doi.org/10.1371/journal.pone.0046233

Neisseria meningitidis, Haemophilus influenzae and Streptococcus pneumoniae are major bacterial agents of meningitis. They each bind the 37/67-kDa laminin receptor (LamR) via the surface protein adhesins: meningococcal PilQ and PorA, H. influenzae Om... Read More about Mapping the laminin receptor binding domains of Neisseria meningitidis PorA and Haemophilus influenzae OmpP2.

The moonlighting protein fructose-1, 6-bisphosphate aldolase of Neisseria meningitidis: Surface localization and role in host cell adhesion (2010)
Journal Article
Tunio, S. A., Oldfield, N. J., Berry, A., Ala'Aldeen, D. A. A., Wooldridge, K. G., & Turner, D. P. J. (2010). The moonlighting protein fructose-1, 6-bisphosphate aldolase of Neisseria meningitidis: Surface localization and role in host cell adhesion. Molecular Microbiology, 76(3), 605-615. https://doi.org/10.1111/j.1365-2958.2010.07098.x

Fructose-1, 6-bisphosphate aldolases (FBA) are cytoplasmic glycolytic enzymes, which despite lacking identifiable secretion signals, have also been found localized to the surface of several bacteria where they bind host molecules and exhibit non-glyc... Read More about The moonlighting protein fructose-1, 6-bisphosphate aldolase of Neisseria meningitidis: Surface localization and role in host cell adhesion.

AasP autotransporter protein of Actinobacillus pleuropneumoniae does not protect pigs against homologous challenge (2009)
Journal Article
Oldfield, N. J., Worrall, K. E., Rycroft, A. N., Ali, T., Wooldridge, K. G., & Ala'Aldeen, D. A. (2009). AasP autotransporter protein of Actinobacillus pleuropneumoniae does not protect pigs against homologous challenge. Vaccine, 27(38), 5278-5283. https://doi.org/10.1016/j.vaccine.2009.06.047

Actinobacillus pleuropneumoniae is a major respiratory pathogen of pigs; current vaccines provide only limited protection. AasP, a subtilisin-like serine protease, is a conserved outer membrane-localised autotransporter protein. We hypothesized that... Read More about AasP autotransporter protein of Actinobacillus pleuropneumoniae does not protect pigs against homologous challenge.

Laminin receptor initiates bacterial contact with the blood brain barrier in experimental meningitis models (2009)
Journal Article
Orihuela, C. J., Mahdavi, J., Thornton, J., Mann, B., Wooldridge, K. G., Abouseada, N., …Tuomanen, E. I. (2009). Laminin receptor initiates bacterial contact with the blood brain barrier in experimental meningitis models. Journal of Clinical Investigation, 119(6), 1638-1646. https://doi.org/10.1172/JCI36759

A diverse array of infectious agents, including prions and certain neurotropic viruses, bind to the laminin receptor (LR), and this determines tropism to the CNS. Bacterial meningitis in childhood is almost exclusively caused by the respiratory tract... Read More about Laminin receptor initiates bacterial contact with the blood brain barrier in experimental meningitis models.

Functional Characterization of AasP, a Maturation Protease Autotransporter Protein of Actinobacillus pleuropneumoniae (2008)
Journal Article
Ali, T., Oldfield, N. J., Wooldridge, K. G., Turner, D. P., & Ala'Aldeen, D. A. A. (2008). Functional Characterization of AasP, a Maturation Protease Autotransporter Protein of Actinobacillus pleuropneumoniae. Infection and Immunity, 76(12), 5608-5614. https://doi.org/10.1128/IAI.00085-08

Actinobacillus pleuropneumoniae is the etiological agent of porcine pleuropneumonia, a highly contagious respiratory infection in pigs. AasP, a putative subtilisin-like serine protease autotransporter, has recently been identified in A. pleuropneumon... Read More about Functional Characterization of AasP, a Maturation Protease Autotransporter Protein of Actinobacillus pleuropneumoniae.

Identification and characterization of novel antigenic vaccine candidates of Actinobacillus pleuropneumoniae (2008)
Journal Article
Oldfield, N. J., Donovan, E. A., Worrall, K. E., Wooldridge, K. G., Langford, P. R., Rycroft, A. N., & Ala'Aldeen, D. A. (2008). Identification and characterization of novel antigenic vaccine candidates of Actinobacillus pleuropneumoniae. Vaccine, 26(16), 1942-1954. https://doi.org/10.1016/j.vaccine.2008.02.022

Actinobacillus pleuropneumoniae is an important respiratory pathogen of swine, for which there is no highly effective vaccine. A phage expression library of the A. pleuropneumoniae genome was constructed and screened to identify potential vaccine com... Read More about Identification and characterization of novel antigenic vaccine candidates of Actinobacillus pleuropneumoniae.

CapA, an Autotransporter Protein of Campylobacter jejuni, Mediates Association with Human Epithelial Cells and Colonization of the Chicken Gut (2007)
Journal Article
Ashgar, S. S., Oldfield, N. J., Wooldridge, K. G., Jones, M. A., Irving, G. J., Turner, D. P., & Ala'Aldeen, D. A. (2007). CapA, an Autotransporter Protein of Campylobacter jejuni, Mediates Association with Human Epithelial Cells and Colonization of the Chicken Gut. Journal of Bacteriology, 189(5), 1856-1865. https://doi.org/10.1128/JB.01427-06

Two putative autotransporter proteins, CapA and CapB, were identified in silico from the genome sequence of Campylobacter jejuni NCTC11168. The genes encoding each protein contain homopolymeric tracts, suggestive of phase variation mediated by a slip... Read More about CapA, an Autotransporter Protein of Campylobacter jejuni, Mediates Association with Human Epithelial Cells and Colonization of the Chicken Gut.

T-cell stimulating protein A (TspA) of Neisseria meningitidis is required for optimal adhesion to human cells (2006)
Journal Article
Oldfield, N. J., Bland, S. J., Taraktsoglou, M., Dos Ramos, F. J., Robinson, K., Wooldridge, K. G., & Ala'Aldeen, D. A. (2007). T-cell stimulating protein A (TspA) of Neisseria meningitidis is required for optimal adhesion to human cells. Cellular Microbiology, 9(2), 463-478. https://doi.org/10.1111/j.1462-5822.2006.00803.x

T-cell stimulating protein A (TspA) is an immunogenic, T-cell and B-cell stimulating protein of Neisseria meningitidis. Sequence similarity between TspA and FimV, a Pseudomonas aeruginosa protein involved in twitching motility, suggested a link betwe... Read More about T-cell stimulating protein A (TspA) of Neisseria meningitidis is required for optimal adhesion to human cells.