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 most commonly recognized examples of moonlighting proteins. Fructose-1,6-bisphosphate aldolase (FBA) is an enzyme involved in the Embden-Meyerhof-Parnas (EMP) glycolytic pathway and in gluconeogenesis. Increasingly, it is also recognized that FBA has additional functions beyond its housekeeping role in central metabolism. In the present review, we summarize the current knowledge of the moonlighting functions of FBA in bacteria.

Urinary tract infection (UTI) is increasingly rising in Bangladesh due to the development of resistance of causative pathogens against commonly prescribed antibiotics. Present study attempted to examine the prevalence of such uropathogens and their antibiogram profiles. Among 462 urine samples collected from patients with UTI, 100 were found to be culture positive. Escherichia coli (70%) was predominating, while Klebsiella spp. (11%) and Enterococcus spp. (6%) were also prevalent. About 96% uropathogens were sensitive against imipenem, and 75% against amikacin.The resistance rate of E. coli and Klebsiella spp. against ampicillin was 98.5 and 100%, respectively, and to cefotaxime, 84.3 and 72.8%, respectively. More than 80% resistance against these antibiotics was scored for other isolates. The frequency of drug resistance was found to be comparatively elevated in E. coli, Pseudomonas spp. and Proteus spp. Overall, the present investigation emphasized the need for routine screening of antibiotic resistance to promote effective medication against UTI.

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 organism invade and survive in the bloodstream leading to disease. Moonlighting proteins perform two or more autonomous, often dissimilar, functions using a single polypeptide chain. They have been increasingly reported on the surface of both prokaryotic and eukaryotic organisms and shown to interact with a variety of host ligands. In some organisms moonlighting proteins perform virulence‐related functions, and they may play a role in the pathogenesis of N. meningitidis. Fructose‐1,6‐bisphosphate aldolase (FBA) was previously shown to be surface‐exposed in meningococci and involved in adhesion to host cells. In this study, FBA was shown to be present on the surface of both pathogenic and commensal neisseriae, and surface localization and anchoring was demonstrated to be independent of aldolase activity. Importantly, meningococcal FBA was found to bind to human glu‐plasminogen in a dose‐dependent manner. Site‐directed mutagenesis demonstrated that the C‐terminal lysine residue of FBA was required for this interaction, whereas subterminal lysine residues were not involved.

Escherichia coli is a pathogen commonly encountered in clinical laboratories, and is capable of causing a variety of diseases, both within the intestinal tract (intestinal pathogenic strains) and outside (extraintestinal pathogenic E. coli , or ExPEC). It is associated with urinary tract infections (UTIs), one of the most common infectious diseases in the world. This report represents the first comparative analysis of the draft genome sequences of 11 uropathogenic E. coli (UPEC) strains isolated from two tertiary hospitals located in Dhaka and Sylhet, Bangladesh, and is focused on comparing their genomic characteristics to each other and to other available UPEC strains. Multilocus sequence typing (MLST) confirmed the strains belong to ST59, ST131, ST219, ST361, ST410, ST448 and ST4204, with one of the isolates classified as a previously undocumented ST. De novo identification of the antibiotic resistance genes bla NDM-5 , bla NDM-7 , bla CTX-M-15 and bla OXA-1 was determined, and phenotypic-genotypic analysis of virulence revealed significant heterogeneity within UPEC phylogroups.

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