Multidrug-Resistant and Extremely Drug-Resistant in Clinical Samples From a Tertiary Healthcare Facility in Nigeria.

Objectives: has been globally implicated in healthcare-associated infection. The susceptibility pattern of clinical isolates of to anti-pseudomonal antibiotics is reported.

Materials And Methods: Clinical samples, namely blood, urine, tracheal aspirate, cerebrospinal fluid (CSF), wound swabs, high vaginal swabs, eye, and ear exudates were obtained from patients, processed and identified using standard microbiological protocols.

Application of a Neisseria meningitidis antigen microarray to identify candidate vaccine proteins from a human Phase I clinical trial.

Meningococcal meningitis is a rare but serious condition affecting mainly children and young adults. Outer membrane vesicles (OMV) from Neisseria meningitidis have been used successfully as vaccines against the disease, although they only provide protection against a limited number of the many existing variants. There have been many attempts to identify suitable protein antigens for use in defined vaccines that provide broad protection against the disease, such as that leading to the development of the four component 4CMenB vaccine.

Immunogenicity profiling of protein antigens from capsular group B Neisseria meningitidis.

Outer membrane vesicle (OMV)- based vaccines have been used to provide strain-specific protection against capsular group B Neisseria meningitidis infections, but the full breadth of the immune response against the components of the OMV has not been established. Sera from adults vaccinated with an OMV vaccine were used to screen 91 outer membrane proteins (OMPs) incorporated in an antigen microarray panel. Antigen-specific IgG levels were quantified pre-vaccination, and after 12 and 18 weeks.

Structure of the Neisseria Adhesin Complex Protein (ACP) and its role as a novel lysozyme inhibitor.

Pathogenic and commensal Neisseria species produce an Adhesin Complex Protein, which was first characterised in Neisseria meningitidis (Nm) as a novel surface-exposed adhesin with vaccine potential. In the current study, the crystal structure of a recombinant (r)Nm-ACP Type I protein was determined to 1.4 Å resolution: the fold resembles an eight-stranded β-barrel, stabilized by a disulphide bond between the first (Cys38) and last (Cys121) β-strands.