Cattle are a potential reservoir of bubaline herpesvirus 1 (BuHV1).

In the present work, controlled experimental infection and transmission studies in domestic cattle (Bos taurus) and water buffaloes (Bubalus bubalis) were carried out to study the in vivo behaviour of bubaline herpesvirus 1 (BuHV1). Two bovine and two buffalo calves were infected with BuHV1 (20287N isolate) by intranasal aerosolisation. Two sentinel cattle did not receive the virus challenge, but were housed with infected buffaloes to evaluate horizontal transmission. All experimentally inoculated animals showed viral infection and respiratory clinical signs. BuHV1 experimentally infected calves showed intermittent viral excretion between 2 days and 18 days postinfection (dpi) with a maximum titre of excretion of 106 TCID50/ml and moderate rhinitis between 2 dpi and 20 dpi. BuHV1 experimentally inoculated buffaloes showed mild respiratory signs, which consisted mainly of serous nasal secretions during the infection period. Sentinel calves showed mucosal specific IgG1 antibodies at seven days postcontact. Viral DNA was detected by PCR and sequencing in both buffaloes and sentinel calves, which could be associated with latency. In conclusion, this study showed the susceptibility of cattle to BuHV1 after both experimental infection and contact with infected buffaloes. These data increase the scarce knowledge on the pathogenesis in natural host and the susceptibility of cattle to BuHV1 experimental infection.

6-Acylamino-2-1[(ethylsulfonyl)oxy]-1H-isoindole-1,3-diones mechanism-based inhibitors of human leukocyte elastase and cathepsin G: effect of chirality in the 6-acylamino substituent on inhibitory potency and selectivity.

Inhibition of human leukocyte elastase(HLE) by a series of 6-acylamino-2-[(ethylsulfonyl)oxy)]-1H-isoindole-1,3-diones was determined and compared to their inhibition of ChT, PPE, and Cat G. The best inhibitor of the series was 6-((1'S)-camphanyl)amino-2-[(ethylsulfonyl) oxy]-1H-isoindole-1,3-dione 5b, with a k(obs)/[I] = 11,000 M(-1) s(-1). This study revealed that HLE shows a preference for the S stereochemistry and tolerates hydrophobic substituents in the Sn' binding sites. Molecular modeling of non-covalent HLE-inhibitor complexes was used as a tool to investigate our binding model. Buffer stability assays reveal that these compounds are susceptible to hydrolysis at physiological pH.