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Role of β−lactamase in the susceptibility of clinical isolates to β−lactam antibiotics Soebandrio, A.; Sri-Budayanti, N. N.; Widayati, A.; Wiwing, V.; Nusatya, M. A.C.M.
Medical Journal of Indonesia Vol 13, No 3 (2004): July-September
Publisher : Faculty of Medicine Universitas Indonesia

Show Abstract | Download Original | Original Source | Check in Google Scholar | Full PDF (181.679 KB) | DOI: 10.13181/mji.v13i3.147

Abstract

Combination of β−lactam antibiotic with β−lactamase inhibitor has been proven to overcome resistance caused by β−lactamase production. An evaluation to the MIC of some β−lactam antibiotics to β−lactamase producing isolates will be reported. A. anitratus, E. coli, K. pneumoniae, Proteus sp, Pseudomonas sp, S. aureus, S. epidermidis, S. pneumoniae, S. viridans, and β−hemolytic Streptococcus, were challenged to Ampicillin/Sulbactam (AMS), Amoxicillin/Clavulanic acid (AMC), Cefoperazone (CFP), Cefoperazone/Sulbactam (CSL), Ceftriaxone (CRO), dan Cefotaxime (CTX) using ETest techniques. β−lactamase production was identified using Cefinase disk. Sixtyfour percent of isolates were capable of producing β−lactamase. All E. coli and K. pneumoniae tested were β−lactamase producer, none of Proteus sp, Pseudomonas sp, and S. epidermidis tested produced β−lactamase. In β−lactamase producing group, Sulbactam was able to reduce resistance to CFP from 25% to 5%. About 20% of β−lactamase producing isolates which were resistant to CFP, were susceptible to CSL. Susceptibility of S.viridans to AMS, AMC, CFP, and CSL was higher than 80%, but less than 50% to CRO and CTX. S. pneumoniae was less susceptible to tested antibiotics, 50 to 60% susceptibility was shown to AMC, CFP, and CSL. S.aureus was 60 to 70% susceptible, while β−haemolytic Streptococcus showed good response to the tested antibiotics. Only 30% or less of K. pneumoniae and E. coli was susceptible to AMS and AMC. A. anitratus showed good susceptibility only to AMS (78%) and CSL (89%). Sixtyfour percent of isolate studied produced β−lactamase. β−lactamase inhibitor could reduce resistance of β−lactamase producing organism to β−lactam antibiotic from 25 to 5 percent. (Med J Indones 2004; 13: 140-5)Keywords: Antibiotic Susceptibility, MIC, β−lactam antibiotic, β−lactamase inhibitor
Potential of Neuraminidase from Pasteurella multocida for Inhibiting Avian Influenza Virus Subtype H9N2 Replication In Ovo Poetri, O. N.; Nugroho, C. M. H.; Silaen, O. S. M.; Kurnia, R. S.; Krisnamurti, D. G. B.; Indrawati, A.; Hikmah, N.; Hariyadi, I. P. P. K.; Putra, M. A.; Soebandrio, A.
Tropical Animal Science Journal Vol. 46 No. 4 (2023): Tropical Animal Science Journal
Publisher : Faculty of Animal Science, Bogor Agricultural University

Show Abstract | Download Original | Original Source | Check in Google Scholar | DOI: 10.5398/tasj.2023.46.4.487

Abstract

In recent decades, neuraminidase/sialidase-based antivirals have been produced to suppress respiratory viral infections, including avian influenza, which relies on sialic acid as the entry point for viruses into cells. While neuraminidase has been extensively studied as an antiviral agent, numerous neuraminidases still have not been evaluated for their antiviral activities. Among these is NanB neuraminidase derived from Pasteurella multocida, which has received limited research attention. This study aimed to assess the potential of NanB neuraminidase in inhibiting H9N2 avian influenza virus infection in ovo. The research commenced with the molecular re-identification of the H9N2 A/Layer/Indonesia/WestJava-04/17 virus isolate, followed by determining the EID50 through Rapid HA test results. The toxicity of NanB neuraminidase was assessed by administering various doses to embryonated chicken eggs (ECE). The antiviral activity of NanB neuraminidase on ECE was evaluated through challenge tests, including treatment before, during, and after the challenge. The assessment involved monitoring the time of embryo death, virus titer through HA test, and viral copy number via RT-qPCR. The results indicated that the H9N2 virus titers capable of infecting 50% of ECE amounted to 108.83 EID50/mL. A dose of 0.258 U/mL of NanB neuraminidase was found to be toxic, leading to embryo mortality after 48 hours of incubation at 37 ℃, while a non-toxic dose was determined to be 0.129 U/mL. The post-challenge treatment group exhibited the most significant reduction in virus titer in ECE. Notably, NanB neuraminidase derived from P. multocida demonstrated the ability to inhibit H9N2 avian influenza virus infection in the ovo model, with the optimal dosage of 0.129 U/mL. The observed decrease in virus titers in the hemagglutination assay and viral copy number assays suggests that NanB neuraminidase holds promise as a potential antiviral candidate for therapeutic approach.