Overview of Canine Babesiosis

Canine babesiosis is a tick-borne, protozoal, haemoparasitic disease that can cause varying degrees of haemolytic anaemia, splenomegaly, thrombocytopenia and fever. There are two hosts for the transmission of Babesia spp., viz. invertebrate (tick) and vertebrate host. Dogs are one among the many targets of Babesia spp., causing canine babesiosis, and now there are clinical evidences of possible vertical transmission too. Dogs of all ages can be affected with Babesia spp., but young puppies are more commonly affected. Considering advanced diagnostic techniques, for an early and specific detection of acute infections, an AgELISA that is potentially translatable to a rapid diagnostic test design is reported. Different molecular techniques used for identification and differentiation of the various species of Babesia are semi-nested PCR, reverse line blotting and PCR-restriction fragment length polymorphism analysis. Treatment consists of three components: treatment with antiprotozoal agents to eliminate the parasite, blood transfusions to treat severe anaemia and supportive care for the complications and metabolic derangements. Blood lactate concentrations can serve as a prognostic indicator in severe or complicated canine babesiosis. For prevention apart from conventional measures, vaccines against Babesia species such as B. gibsoni are currently being developed

ABC Transporter Genes Show Upregulated Expression in Drug Resistant Clinical Isolates of Candida auris : a Genome-Wide Characterization of ATP-Binding Cassette (ABC) Transporter Genes

Funding This work was supported by the ICMR (AMR/149/2018-ECD-II) and DBT (BT/PR14117/BRB/10/1420/2015) to RP. AKM appreciates the support by research grant EMR/2016/001927 and DST PURSE II from the Department of Science and Technology (IN). MW was grateful for a Senior Research Fellowship from the University Grant Commission. NG acknowledges the Wellcome Trust support of a Senior Investigator (101873/Z/13/Z), Collaborative (200208/A/15/Z), and Strategic Awards (097377/Z11/Z), and the MRC Centre for Medical Mycology (MR/N006364/1). AJM was supported by the University of Aberdeen studentship. Work in AL’s laboratory was supported by the Wellcome Trust (212524/Z/18/Z) and the Medical Research Council (MRC) Centre for Medical Mycology at the University of Aberdeen (MR/P501955/1 and MR/N006364/1). Acknowledgments We thank the Centre for Genome Enabled Biology and Medicine at the University of Aberdeen (E. Collie-Duguid and S. Shaw) for sequencing and support with genome analysis.Peer reviewedPublisher PD

The Clinical Efficacy and Safety of Acepromazine and Propofol Anesthesia for the Cesarean Section in the Cat

A 3-year-old crossbred cat was presented at the clinics. History revealed that the cat had sustained frequent straining for the last 12 hrs. One kitten was found stuck in the birth canal. The cat was premedicated with atropine sulphate @ 0.04 mg/kg b.wt and tranquilized with acepromazine maleate @ 0.1mg/kg b.wt. I/M, and anesthetized with propofol @ 4 mg/kg b.wt. I/V. via the cephalic vein. The abdominal region was aseptically prepared from the umbilicus to the pubis region. A ventral mid line incision of approximately 3.5 cm was made in linea alba between the umbilicus and pubis, caudally. The gravid uterus was exposed through the surgical wound. A longitudinal incision was placed on the uterine body and kittens were taken out slowly one by one. One of the kittens, which was stuck in the vaginal orifice, was taken out slowly by gently manipulating its presentation. A total of four kittens were born. The use of acepromazine and propofol anesthesia for the cesarean section in the cat proved to be an easy and excellent method without any complications. [Arch Clin Exp Surg 2012; 1(4.000): 258-260

Elucidation of stable intermediates in urea-induced unfolding pathway of human carbonic anhydrase IX

<p>Human carbonic anhydrase IX (CAIX) has evolved as a promising biomarker for cancer prognosis, due to its overexpression in various cancers and restricted expression in normal tissue. However, limited information is available on its biophysical behavior. The unfolding of CAIX in aqueous urea solution was studied using all-atom molecular dynamics simulation approach. The results of this study revealed a stable intermediate state along the unfolding pathway of CAIX. At intermediate concentrations of urea (2.0–4.0 M), the protein displays a native-like structure with a large population of its secondary structure and hydrophobic contacts remaining intact in addition to small confined overall motions. Beyond 4.0 M urea, the unfolding is more gradual and at 8.0 M urea the structure is largely collapsed due to the solvent effect. The hydrophobic contact analysis suggests that the contact in terminal α-helices is separated initially which propagates in the loss of contacts from centrally located β-sheets. The reduction of 60–65% tertiary contacts in 7.0–8.0 M urea suggested the presence of residual structure in unfolded state and is confirmed with structural snap shot. Free energy landscape analysis suggested that unfolding of CAIX exists through the different intermediate states.</p

Multi-omics approaches for remediation of bisphenol A: Toxicity, risk analysis, road blocks and research perspectives

In this &quot;plastic era&quot; with the increased use of plastic in day today&apos;s life the accumulation of its degraded products like microplastics or plastic additives such as Bisphenol A(BPA) is also increasing. BPA is an endocrine-disrupting chemical used as a plasticizing agent in clear plastic, building materials, coatings, and epoxy resin. Several enzymes including laccases and lipases have been studied for the reduction of BPA toxicity. Over the decades of encountering these toxicants, microorganisms have evolved to degrade different classes of plastic additives. Since the degradation of BPA is a long process thus meta-omics approaches have been employed to identify the active microbiota and microbial dynamics involved in the mitigation of BPA. It is also necessary to investigate the impact of processing activities on transit of BPA in food items and to limit its entrance in food world. This review summarizes a comprehensive overview on BPA sources, toxicity, bio-based mitigation approaches along with a deeper understanding of multi-omics approaches for its reduction and risk analysis. Knowledge gaps and op-portunities have been comprehensively compiled that would aid the state-of-the-art information in the available literature for the researchers to further address this issue

V_HH Structural Modelling Approaches: A Critical Review

VHH, i.e., VH domains of camelid single-chain antibodies, are very promising therapeutic agents due to their significant physicochemical advantages compared to classical mammalian antibodies. The number of experimentally solved VHH structures has significantly improved recently, which is of great help, because it offers the ability to directly work on 3D structures to humanise or improve them. Unfortunately, most VHHs do not have 3D structures. Thus, it is essential to find alternative ways to get structural information. The methods of structure prediction from the primary amino acid sequence appear essential to bypass this limitation. This review presents the most extensive overview of structure prediction methods applied for the 3D modelling of a given VHH sequence (a total of 21). Besides the historical overview, it aims at showing how model software programs have been shaping the structural predictions of VHHs. A brief explanation of each methodology is supplied, and pertinent examples of their usage are provided. Finally, we present a structure prediction case study of a recently solved VHH structure. According to some recent studies and the present analysis, AlphaFold 2 and NanoNet appear to be the best tools to predict a structural model of VHH from its sequence

Solvent sensitivity of protein aggregation in Cu, Zn superoxide dismutase: a molecular dynamics simulation study

<p>Misfolding and aggregation of Cu, Zn Superoxide Dismutase (SOD1) is often found in amyotrophic lateral sclerosis (ALS) patients. The central apo SOD1 barrel was involved in protein maturation and pathological aggregation in ALS. In this work, we employed atomistic molecular dynamics (MD) simulations to study the conformational dynamics of SOD1^barrel monomer in different concentrations of trifluoroethanol (TFE). We find concentration dependence unusual structural and dynamical features, characterized by the local unfolding of SOD1^barrel. This partially unfolded structure is characterized by the exposure of hydrophobic core, is highly dynamic in nature, and is the precursor of aggregation seen in SOD1^barrel. Our computational studies supports the hypothesis of the formation of aggregation ‘building blocks’ by means of local unfolding of apo monomer as the mechanism of SOD1 fibrillar aggregation. The non-monotonic TFE concentration dependence of protein conformational changes was explored through simulation studies. Our results suggest that altered protein conformation and dynamics within its structure may underlie the aggregation of SOD1 in ALS.</p

ABC transportome inventory of human pathogenic yeast Candida glabrata: Phylogenetic and expression analysis.

ATP-binding cassette (ABC) is one of the two major superfamilies of transporters present across the evolutionary scale. ABC superfamily members came to prominence due to their ability to extrude broad spectrum of substrates and to confer multi drug resistance (MDR). Overexpression of some ABC transporters in clinical isolates of Candida species was attributed to the development of MDR phenotypes. Among Candida species, Candida glabrata is an emerging drug resistant species in human fungal infections. A comprehensive analysis of such proteins in C. glabrata is required to untangle their role not only in MDR but also in other biological processes. Bioinformatic analysis of proteins encoded by genome of human pathogenic yeast C. glabrata identified 25 putative ABC protein coding genes. On the basis of phylogenetic analysis, domain organization and nomenclature adopted by the Human Genome Organization (HUGO) scheme, these proteins were categorized into six subfamilies such as Pleiotropic Drug Resistance (PDR)/ABCG, Multi Drug Resistance (MDR)/ABCB, Multi Drug Resistance associated Protein (MRP)/ABCC, Adrenoleukodystrophy protein (ALDp)/ABCD, RNase L Inhibitor (RLI)/ABCE and Elongation Factor 3 (EF3)/ABCF. Among these, only 18 ABC proteins contained transmembrane domains (TMDs) and were grouped as membrane proteins, predominantly belonging to PDR, MDR, MRP, and ALDp subfamilies. A comparative phylogenetic analysis of these ABC proteins with other yeast species revealed their orthologous relationship and pointed towards their conserved functions. Quantitative real time PCR (qRT-PCR) analysis of putative membrane localized ABC protein encoding genes of C. glabrata confirmed their basal expression and showed variable transcriptional response towards antimycotic drugs. This study presents first comprehensive overview of ABC superfamily proteins of a human fungal pathogen C. glabrata, which is expected to provide an important platform for in depth analysis of their physiological relevance in cellular processes and drug resistance