Search

This study was conducted to provide structural and morphological data on the sacra of greyhounds. Descriptive quantitative investigation was carried out on 171 sacra of greyhound`s cadavers and then classified into standard and fused sacra based on the number of fused sacral vertebrae. The weight, length and width of sacrum of sacra were measured. Both standard (59%) and fused sacra (41%) were identified. The average length and width of the standard sacrum were found to be 46.14 ± 2.53 mm and 57.89 ± 3.54 mm, respectively. The sacral length was 1.61-mm longer in males (p < .01), and the sacral width was 0.46-mm shorter in males but not significant (p = .51). The average weight of a standard sacrum was 26.54 ± 4.55 g and was 1.18 g heavier in males but not statistically significant (p = .24). Results showed that one-kilogram increase in the body mass was associated with a 0.3 mm (p < .001) increase in sacral length, and a 0.54 mm (p < .001) increase in sacral width, respectively. The morphological data of the standard and fused sacra provided in this study might help the veterinary community to improve treatment and rehabilitation and help the trainer to design the right training protocol for racing greyhounds. In addition, the results of this study are a step to understand the sacrum's functions and how the greyhound's body functions and future studies are required to investigate the biological importance of these findings., (© 2021 Wiley-VCH GmbH.)

Mycoplasma bovis causes serious infections in ruminants, leading to huge economic losses. Lipoproteins are key components of the mycoplasma membrane and are believed to function in nutrient acquisition, adherence, enzymatic interactions with the host, and induction of the host's immune response to infection. Many genes of M. bovis have not been assigned functions, in part because of their low sequence similarity with other bacteria, making it difficult to extrapolate gene functions. This study examined functions of a surface-localized leucine-rich repeat (LRR) lipoprotein encoded by mbfN of M. bovis PG45. Homologs of MbfN were detected as 48-kDa peptides by Western blotting in all the strains of M. bovis included in this study, with the predicted 70-kDa full-length polypeptide detected in some strains. Sequence analysis of the gene revealed the absence in some strains of a region encoding the carboxyl-terminal 147 amino acids found in strain PG45, which could account for the variation detected by immunoblotting. In silico analysis of MbfN suggested that it may have an adhesion-related function. In vitro binding assays confirmed MbfN to be a fibronectin and heparin-binding protein. Disruption of mbfN in M. bovis PG45 significantly reduced ( P = 0.033) the adherence of M. bovis PG45 to MDBK cells in vitro , demonstrating the role of MbfN as an adhesin. IMPORTANCE Experimental validation of the putative functions of genes in M. bovis will advance our understanding of the basic biology of this economically important pathogen and is crucial in developing prevention strategies. This study demonstrated the extracellular matrix binding ability of a novel immunogenic lipoprotein of M. bovis , and the role of this protein in adhesion by M. bovis suggests that it could play a role in virulence., (Copyright © 2020 American Society for Microbiology.)

The survival, replication, and virulence of mycoplasmas depend on their ability to capture and import host-derived nutrients using poorly characterized membrane proteins. Previous studies on the important bovine pathogen Mycoplasma bovis demonstrated that the amino-terminal end of an immunogenic 226-kDa (P226) protein, encoded by milA (the full-length product of which has a predicted molecular weight of 303 kDa), had lipase activity. The predicted sequence of MilA contains glycosaminoglycan binding motifs, as well as multiple copies of a domain of unknown function (DUF445) that is also found in apolipoproteins. We mutagenized the gene to facilitate expression of a series of regions spanning the gene in Escherichia coli Using monospecific antibodies against these recombinant proteins, we showed that MilA was proteolytically processed into 226-kDa and 50-kDa fragments that were both partitioned into the detergent phase by Triton X-114 phase fractionation. Trypsin treatment of intact cells showed that P226 was surface exposed. In vitro , the recombinant regions of MilA bound to 1-anilinonaphthalene-8-sulfonic acid and to a variety of lipids. The MilA fragments were also shown to bind heparin. Antibody against the carboxyl-terminal fragment inhibited the growth of M. bovis in vitro This carboxyl end also bound and hydrolyzed ATP, suggestive of a potential role as an autotransporter. Our studies have demonstrated that DUF445 has lipid binding activity and that MilA is a multifunctional protein that may play multiple roles in the pathogenesis of infection with M. bovis ., (Copyright © 2020 American Society for Microbiology.)

Mycoplasma membrane proteins influence cell shape, cell division, motility and adhesion to host cells, and are thought to be integrally involved in the pathogenesis of mycoplasmoses. Many of the membrane proteins predicted from mycoplasma genome sequences remain hypothetical, as their presence in cellular protein preparations is yet to be established experimentally. Recent genome sequences of several strains of Mycoplasma bovis have provided further insight into the potential role of the membrane proteins of this pathogen in colonisation and infection. This review highlights recent advances in knowledge about the influence of M. bovis membrane proteins on the pathogenesis of infection with this species and identifies future research directions for enhancing our understanding of the role of these proteins., (Copyright © 2013 Elsevier Ltd. All rights reserved.)