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Ticks and tick-borne disease (TBD) are major challenges to cattle production in the tropics and subtropics. Economic losses associated with ticks amount to billions of dollars annually. Although efforts to eradicate ticks and TBD using chemical control strategies have been implemented in many developing countries for decades, these acaricides are costly, and cattle susceptibility to ticks remains unchanged. Traditional breeding methods, where the farmer selected animals using records to improve the host genetic resistance to ticks (HGRT), are less than fully effective and time consuming. The HGRT has been reported in literature. To date, solutions to fight ticks and TBD are still unclear. Development of single-nucleotide polymorphism (SNP) technologies has created an opportunity to estimate breeding values of animals from DNA samples. The use of SNP technology for genomic selection allows information retrieval from the genotype even before the gene is expressed; thus potentially giving farmers the ability to make selection decisions on HGRT at an earlier age. This review discusses factors that affect HGRT, breeding selection, immunology, and genomic approaches and their application to improve HGRT in order to enhance livestock production.

Many beta-lactamases have active-site serine residues, and are competitively inhibited by boronic acids. Hitherto, the boronic acids used have lacked any structural resemblance to the substrates of beta-lactamases. Phenylacetamidomethaneboronic acid, trifluoroacetamidomethaneboronic acid and 2,6-dimethoxybenzamidomethaneboronic acid have now been synthesized. The first of these contains the side-chain moiety of penicillin G, and the last that of methicillin. The pH-dependence of binding of the first inhibitor to beta-lactamase I from Bacillus cereus revealed pK values of 4.7 and 8.2 for (presumably) active-site groups in the enzyme. The kinetics of inhibition were studied by cryoenzymology and by stopped-flow spectrophotometry. These techniques provided evidence for a two-step mechanism of binding of the first two boronic acids mentioned above to beta-lactamase I, and for benzeneboronic acid to a beta-lactamase from Pseudomonas aeruginosa. The slower step is probably associated with a change in enzyme conformation as well as the formation of an O-B bond between the active-site serine hydroxy group and the boronic acid.

D‐(‐)‐Penicillamine (I) is subjected to cyclocondensation with glycolaldehyde (II) in hot aqueous methanol to form the diastereomeric thiazolidines (III) and (IV) which are converted into the benzylic esters (VI) and (VII) via the corresponding cesium salts.