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Copyright of Revista Veterinaria is the property of Universidad Nacional del Nordeste and its content may not be copied or emailed to multiple sites or posted to a listserv without the copyright holder's express written permission. However, users may print, download, or email articles for individual use. This abstract may be abridged. No warranty is given about the accuracy of the copy. Users should refer to the original published version of the material for the full abstract. (Copyright applies to all Abstracts.)

Copyright of BIOAGRO is the property of Revista BIOAGRO and its content may not be copied or emailed to multiple sites or posted to a listserv without the copyright holder's express written permission. However, users may print, download, or email articles for individual use. This abstract may be abridged. No warranty is given about the accuracy of the copy. Users should refer to the original published version of the material for the full abstract. (Copyright applies to all Abstracts.)

Mannose-binding lectin (MBL) is a protein whose gen (MBL 2) is in the Iong arm of chromosome 10. Low serum concentrations of this protein may be affected by three genetic variants (B, C, and D) in the structural portion of the MBL 2 gen and to additional variations in the promoter region of it, which generate two polymorphic sites (H/L and X/Y). These polymorphisms create diverse haplotypes in some human communities that may increase the susceptibility to infections, generalized lupus erythematous and rheumatoid arthritis. This study reviews the MBL 2 gen polymorphisms and its relation with the health of the affected human populations. [ABSTRACT FROM AUTHOR]

Per-O-acetyl-5-thio-DL-mannose was synthesized from petrochemicals in six steps and 9% overall yield. It was then derivatized into glycosyl trichloroacetimidate and subjected to glycosidation reaction with a mannosyl acceptor to give a separatable mixture of disaccharides with 5-thio-D- and L-mannosides. This is the first synthesis of an enantiomerically pure 5-thiosugar derivative from racemic chemicals. The D-glycoside was derivatized intomethyl (5-thio-α-D-mannopyranosyl)-2-O-α-D-mannopyranoside 6-phosphate as a potential inhibitor of a golgi α-1,2-mannosidase. [ABSTRACT FROM AUTHOR]

Live attenuated vaccine candidates of Vibrio cholerae are the most promising option to develop an effective vaccine against cholera disease. However, the releasing to the environment of millions of vibrio cells during vaccination campaigns entails the risk that attenuated strains reacquire the cholera toxin genes by a horizontal gene transfer mechanism. This work describes the construction of a new generation of vaccine candidates with improved environmental safety features by deletion of the mshA gene from the chromosome of the Vibrio cholerae vaccine strains. This gene encodes the main subunit of the mannose sensitive hemagglutinin (MSHA) type 4 pilus, which functions as a receptor of the filamentous phage VGJφ. The phage VGJφ is able to transduce the genes encoding cholera toxin, the main virulence factor of V. cholerae, through a specific and efficient mechanism. Therefore, the MSHA pilus is a port of entry for the genes of cholera toxin by horizontal gene transfer. The strategy used to delete the mshA gene was the genetic replacement of the wild type gene by an internal deleted copy of the gene contained in a suicide vector. The resultant ΔmshA mutants showed full resistance to the infection with VGJφ, thus, they are unable to reacquire the cholera toxin encoding genes through the mechanism mediated by this phage. Besides, these mutants kept unaltered the features of their parental strains that are desirables for an effective vaccine candidate, such as the morphology, growing rate, motility and ability to colonize the small intestine in the suckling mouse cholera model. [ABSTRACT FROM AUTHOR]