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1.
Antibiotics (Basel) ; 11(11)2022 Nov 04.
Article in English | MEDLINE | ID: mdl-36358208

ABSTRACT

Multidrug-resistant (MDR) foodborne pathogens have created a great challenge to the supply and consumption of safe & healthy animal-source foods. The study was conducted to identify the common foodborne pathogens from animal-source foods & by-products with their antimicrobial drug susceptibility and resistance gene profile. The common foodborne pathogens Escherichia coli (E. coli), Salmonella, Streptococcus, Staphylococcus, and Campylobacter species were identified in livestock and poultry food products. The prevalence of foodborne pathogens was found higher in poultry food & by-product compared with livestock (p < 0.05). The antimicrobial drug susceptibility results revealed decreased susceptibility to penicillin, ampicillin, amoxicillin, levofloxacin, ciprofloxacin, tetracycline, neomycin, streptomycin, and sulfamethoxazole-trimethoprim whilst gentamicin was found comparatively more sensitive. Regardless of sources, the overall MDR pattern of E. coli, Salmonella, Staphylococcus, and Streptococcus were found to be 88.33%, 75%, 95%, and 100%, respectively. The genotypic resistance showed a prevalence of blaTEM, blaSHV, blaCMY, tetA, tetB, sul1, aadA1, aac(3)-IV, and ereA resistance genes. The phenotype and genotype resistance patterns of isolated pathogens from livestock and poultry had harmony and good concordance, and sul1 & tetA resistance genes had a higher prevalence. Good agricultural practices along with proper biosecurity may reduce the rampant use of antimicrobial drugs. In addition, proper handling, processing, storage, and transportation of foods may decline the spread of MDR foodborne pathogens in the food chain.

2.
Parasitol Int ; 64(5): 389-91, 2015 Oct.
Article in English | MEDLINE | ID: mdl-26028431

ABSTRACT

We investigated the presence of antibodies against Toxoplasma gondii in domesticated goats intended for human consumption in a rural suburb of Rajshahi, Bangladesh. Antibodies to T. gondii were found in 55.1% (80/145) of the goats tested in our sample. The seroprevalence among goats aged <1 year, 1-2 years, 2-3 years and ≥3 years were 36.7%, 66.0%, 59.1% and 100%, respectively. Our results demonstrated that seroprevalence increased with age. Among the seropositive goats, a subsample of eight free-ranging female goats with access to male goats was placed under continuous observation. During the observation period, these seropositive female goats delivered 11 kids, all of which were found to be seronegative before suckling colostrum. This finding strongly suggested that trans-placental infection rarely occurs in female goats that have acquired an infection before pregnancy. Our results indicate that infection via ingestion of oocysts plays a more important role than endogenous trans-placental infection in maintaining the endemicity of T. gondii among goats in Bangladesh.


Subject(s)
Antibodies, Protozoan/blood , Infectious Disease Transmission, Vertical/veterinary , Pregnancy Complications, Parasitic/veterinary , Toxoplasma/immunology , Toxoplasmosis, Animal/immunology , Animals , Bangladesh/epidemiology , Female , Male , Pregnancy , Toxoplasmosis, Animal/epidemiology
3.
Proc Natl Acad Sci U S A ; 108(50): 19955-60, 2011 Dec 13.
Article in English | MEDLINE | ID: mdl-22114184

ABSTRACT

V-ATPases function as ATP-dependent ion pumps in various membrane systems of living organisms. ATP hydrolysis causes rotation of the central rotor complex, which is composed of the central axis D subunit and a membrane c ring that are connected by F and d subunits. Here we determined the crystal structure of the DF complex of the prokaryotic V-ATPase of Enterococcus hirae at 2.0-Å resolution. The structure of the D subunit comprised a long left-handed coiled coil with a unique short ß-hairpin region that is effective in stimulating the ATPase activity of V(1)-ATPase by twofold. The F subunit is bound to the middle portion of the D subunit. The C-terminal helix of the F subunit, which was believed to function as a regulatory region by extending into the catalytic A(3)B(3) complex, contributes to tight binding to the D subunit by forming a three-helix bundle. Both D and F subunits are necessary to bind the d subunit that links to the c ring. From these findings, we modeled the entire rotor complex (DFdc ring) of V-ATPase.


Subject(s)
Enterococcus/enzymology , Prokaryotic Cells/enzymology , Protein Subunits/chemistry , Vacuolar Proton-Translocating ATPases/chemistry , Amino Acid Sequence , Crystallography, X-Ray , Models, Molecular , Molecular Sequence Data , Protein Structure, Secondary , Protein Subunits/metabolism , Sequence Alignment , Static Electricity , Structural Homology, Protein , Vacuolar Proton-Translocating ATPases/metabolism
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