11 research outputs found

    Applications of Personalised Phage Therapy highlighting the importance of Bacteriophage Banks against Emerging Antimicrobial Resistance

    Get PDF
    Emerging antibiotic resistance is one of the most important microbiological issues of the 21st century. This poses a query regarding the future use of antibiotics and availability of other promising therapeutic alternatives. The awareness about antibiotic misuse has improved insufficiently and is evident by the increased incidences of multidrug resistant infections globally. Amongst different antibacterial therapeutic approaches phage therapy has created a niche of its own due to continuous use for treatment of human infections in Eastern Europe. Synergistic compounds along with phages have also been proposed as a better alternative compared to antibiotics or phage alone for treatment of chronic cases and seriously debilitating diseases. As such, why not allow custom made phage therapy for treatment of chronic infections? However, the success of phage therapy will depend upon instant availability of characterised bacteriophages from bacteriophage banks which may serve as the major catalyst in bringing Phage Therapy to main stream treatment alternatives or in combination therapy at least. In the current article we present a glimpse of comprehensive approach about utility of bacteriophage banks and further present personalised phage therapy in a synergistic role with antibiotics to overcome emerging antimicrobial resistance

    Not Available

    No full text
    Not AvailableThe present immuno-diagnostic method using soluble antigens from whole cell lysate antigen for trypanosomosis have certain inherent problems like lack of standardized and reproducible antigens, as well as ethical issues due to in vivo production, that could be alleviated by in vitro production. In the present study we have identified heat shock protein 70 (HSP70) from T. evansi proteome. The nucleotide sequence of T. evansi HSP70 was 2116 bp, which encodes 690 amino acid residues. The phylogenetic analysis of T. evansi HSP70 showed that T. evansi occurred within Trypanosoma clade and is most closely related to T. brucei brucei and T. brucei gambiense, whereas T. congolense HSP70 laid in separate clade. The two partial HSP70 sequences (HSP-1 from N-terminal region and HSP-2 from C-terminal region) were expressed and evaluated as diagnostic antigens using experimentally infected equine serum samples. Both recombinant proteins detected antibody in immunoblot using serum samples from experimental infected donkeys with T. evansi. Recombinant HSP-2 showed comparable antibody response to Whole cell lysate (WCL) antigen in immunoblot and ELISA. The initial results indicated that HSP70 has potential to detect the T. evansi infection and needs further validation on large set of equine serum samples.Not Availabl

    Not Available

    No full text
    Not AvailableThe present immuno-diagnostic method using soluble antigens from whole cell lysate antigen for trypanosomosis have certain inherent problems like lack of standardized and reproducible antigens, as well as ethical issues due to in vivo production, that could be alleviated by in vitro production. In the present study we have identified heat shock protein 70 (HSP70) from T. evansi proteome. The nucleotide sequence of T. evansi HSP70 was 2116 bp, which encodes 690 amino acid residues. The phylogenetic analysis of T. evansi HSP70 showed that T. evansi occurred within Trypanosoma clade and is most closely related to T. brucei brucei and T. brucei gambiense, whereas T. congolense HSP70 laid in separate clade. The two partial HSP70 sequences (HSP-1 from N-terminal region and HSP-2 from C-terminal region) were expressed and evaluated as diagnostic antigens using experimentally infected equine serum samples. Both recombinant proteins detected antibody in immunoblot using serum samples from experimental infected donkeys with T. evansi. Recombinant HSP-2 showed comparable antibody response to Whole cell lysate (WCL) antigen in immunoblot and ELISA. The initial results indicated that HSP70 has potential to detect the T. evansi infection and needs further validation on large set of equine serum samples.Not Availabl

    Production and preliminary evaluation of Trypanosoma evansi HSP70 for antibody detection in Equids

    No full text
    The present immuno-diagnostic method using soluble antigens from whole cell lysate antigen for trypanosomosis have certain inherent problems like lack of standardized and reproducible antigens, as well as ethical issues due to in vivo production, that could be alleviated by in vitro production. In the present study we have identified heat shock protein 70 (HSP70) from T. evansi proteome. The nucleotide sequence of T. evansi HSP70 was 2116 bp, which encodes 690 amino acid residues. The phylogenetic analysis of T. evansi HSP70 showed that T. evansi occurred within Trypanosoma clade and is most closely related to T. brucei brucei and T. brucei gambiense, whereas T. congolense HSP70 laid in separate clade. The two partial HSP70 sequences (HSP-1 from N-terminal region and HSP-2 from C-terminal region) were expressed and evaluated as diagnostic antigens using experimentally infected equine serum samples. Both recombinant proteins detected antibody in immunoblot using serum samples from experimental infected donkeys with T. evansi. Recombinant HSP-2 showed comparable antibody response to Whole cell lysate (WCL) antigen in immunoblot and ELISA. The initial results indicated that HSP70 has potential to detect the T. evansi infection and needs further validation on large set of equine serum samples

    <span style="font-size:11.0pt;font-family: "Times New Roman";mso-fareast-font-family:"Times New Roman";mso-bidi-font-family: Mangal;mso-ansi-language:EN-GB;mso-fareast-language:EN-US;mso-bidi-language: HI" lang="EN-GB">Molecular characterization of virulence-associated protein (Vap) family genes of pathogenic <i style="mso-bidi-font-style:normal">Rhodococcus equi</i> isolates from clinical cases of Indian equines</span>

    No full text
    195-202<span style="font-size:9.0pt;mso-ansi-language:EN-IN;mso-bidi-font-weight: bold">Virulence-associated plasmid (Vap) genes of clinical isolates of Rhodococcus equi were characterized. Isolates were identified by 16S rRNA, choE and <i style="mso-bidi-font-style: normal">traA gene PCR, followed by amplification, cloning and sequencing of 7 Vap<span style="mso-bidi-font-weight: bold"> genes. <span style="font-size:9.0pt;mso-ansi-language:EN-IN;mso-bidi-font-weight: bold">The isolates were found positive for <i style="mso-bidi-font-style: normal">vapA gene family. The comparative sequence analysis of vap genes revealed 99-100% similarity at both nt and aa levels with all sequences. The aa sequences of the predicted Vap proteins<span style="font-size: 9.0pt;mso-ansi-language:EN-IN;mso-bidi-font-weight:bold"> exhibited a high degree of similarity to each other, especially at the carboxy terminal ends. Invariable point mutations were observed in Vap proteins<span style="font-size:9.0pt;mso-bidi-font-weight: bold" lang="EN-GB">.<span style="font-size:9.0pt;mso-ansi-language:EN-IN;mso-bidi-font-weight: bold"> The changes did not cause alteration in hydropathicity and secondary structures in VapA & H proteins. Few major changes in polarity and structures were observed in VapD, E and G proteins. Phylogenetic analysis revealed that all <i style="mso-bidi-font-style: normal">Vap genes followed similar branching pattern except isolate from Bahadurgarh (BBG163). <span style="font-size:9.0pt;mso-ansi-language: EN-IN;mso-bidi-font-weight:bold">We conclude that VapA is highly conserved and plays a major role in pathogenesis<span style="font-size:9.0pt;mso-ansi-language: EN-IN;mso-bidi-font-weight:bold">. This is the first report of sequence analysis and phylogenetic studies of Vap gene family of clinical virulent isolates of <i style="mso-bidi-font-style: normal">R. equi from India. </span

    Descriptive epidemiology of equine influenza in India (2008-2009): temporal and spatial trends

    No full text
    Equine influenza is a contagious viral disease that affects all members of the family Equidae, i.e. horses, donkeys and mules. The authors describe the pattern of equine influenza outbreaks in a number of states of India from July 2008 to June 2009. The disease was first reported in June 2008 in Katra (Jammu and Kashmir) and spread to ten other states within a year. All outbreaks of equine influenza in the various states were confirmed by laboratory investigations (virus isolation and/or serological confirmation based on haemagglutination inhibition [HI] assays of paired samples) before declaring them as equine influenza virus-affected state(s). The virus (H3N8) was reported from various locations in the country including Katra, Mysore (Karnataka), Ahmedabad (Gujarat), Gopeshwar and Uttarkashi (Uttarakhand) and was isolated in 9- to 11-day-old embryonated chicken eggs. The virus was confirmed as H3N8 by HI assays with standard serum and amplification of full-length haemagglutinin and neuraminidase genes by reverse transcriptase-polymerase chain reaction. Serum samples (n = 4 740) of equines from 13 states in India screened by HI revealed 1 074 (22.65%) samples as being positive for antibodies to equine influenza virus (H3N8)
    corecore