Displaying all 6 publications

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  1. Ali HM, Mohamed Mustafa MI, Rizal MR, Ng SW
    PMID: 21202476 DOI: 10.1107/S1600536808012968
    The Ni atom in the title compound, [Ni(C(17)H(15)N(2)O)(2)]·2C(3)H(7)NO, lies on a twofold rotation axis. It is N,O-chelated by the deprotonated Schiff base 2-[2-(1H-indol-3-yl)ethyl-imino-meth-yl]phenolate ligand in a square-planar coordination environment. The mol-ecule is linked to a solvent mol-ecule by an indole-dimethyl-formamide N-H⋯O hydrogen bond.
  2. Ali HM, Mohamed Mustafa MI, Rizal MR, Ng SW
    PMID: 21202395 DOI: 10.1107/S1600536808011185
    The title Schiff base, C(17)H(15)N(3)O(3), exists in the zwitterionic form with the phenol H atom transferred to the imine group. Adjacent zwitterions are linked into a linear chain running along the a axis by an indole-hydr-oxy N-H⋯O hydrogen bond [3.100 (2) Å].
  3. Ali HM, Mohamed Mustafa MI, Rizal MR, Ng SW
    PMID: 21201365 DOI: 10.1107/S1600536808002213
    The Zn atom in the title compound, [Zn(C(17)H(14)ClN(2)O)(2)], is N,O-chelated by two deprotonated Schiff base monoanionic ligands in a tetra-hedral coordination geometry. The Zn atom lies on a special position of site symmetry 2.
  4. Ali HM, Mohamed Mustafa MI, Rizal MR, Ng SW
    PMID: 21202245 DOI: 10.1107/S1600536808011161
    In the mononuclear complex mol-ecule of the title compond, [ZnCl(2)(C(18)H(18)N(2)O)(2)]·2C(18)H(18)N(2)O, the Zn atom, which lies on a twofold rotation axis, is coordinated by phenolate O atoms in a tetra-hedral coordination geometry. The coordinated Schiff base uses its indole NH donor site to form a hydrogen bond to the negatively charged phenolate O atom of the uncoordinated zwitterionic Schiff base. There is an intra-molecular N-H⋯O hydrogen bond in the coordinated and uncoordinated Schiff bases. The indole NH site of the uncoordinated Schiff base does not engage in a hydrogen-bond inter-action. The CH(2)-CH(2) group in the uncoordinated Schiff base is disordered equally over two positions.
  5. Mustafa MI, Al-Marzooq F, How SH, Kuan YC, Ng TH
    Trop Biomed, 2011 Dec;28(3):531-44.
    PMID: 22433882 MyJurnal
    Community-acquired pneumonia (CAP) is still a major cause of morbidity and mortality especially to children and compromised hosts, such as the old and those with underlying chronic diseases. Knowledge of pathogens causing CAP constitutes the basis for selection of antimicrobial treatment. Previous data have shown that etiological agents can be identified in only up to 50% of patients, but this figure can be improved by using polymerase chain reaction (PCR). This study was designed to evaluate multiplex real-time PCR as a method for rapid differential detection of five bacterial causes of CAP (Streptococcus pneumoniae, Burkholderia pseudomallei and atypical bacterial pathogens namely Mycoplasma pneumoniae, Chlamydophila pneumoniae and Legionella pneumophila) in CAP patients attending Hospital Tengku Ampuan Afzan (HTAA)/ Kuantan, Pahang, Malaysia. Two previously developed multiplex real-time PCR assays, duplex for the differential detection of S. pneumoniae and B. pseudomallei and triplex for the atypical bacterial pathogens, were used to detect a bacterial cause of CAP in blood and respiratory samples. Thus, 46 blood and 45 respiratory samples collected from 46 adult CAP patients admitted to HTAA were analysed by multiplex real-time PCR assays and conventional methods. The microbial etiology of CAP could be established for 39.1% (18/46) of CAP patients by conventional methods and this was increased to 65.2% (30/46) with the additional use of real-time PCR. The most frequently detected pathogens were S. pneumoniae (21.7% - all by PCR alone), Klebsiella pneumoniae (17.3%), B. pseudomallei (13% - 83% of them positive by PCR alone and 17% by both culture and PCR), Pseudomonas aeruginosa (6.5%), M. pneumoniae (6.5% - all by serology), C. pneumoniae (4.3% - all positive by both PCR and serology), L. pneumophila (2.1% - all by PCR alone), Escherichia coli (4.3%). Haemophilus infuenzae, Acinetobacter lwoffii and Acinetobacter baumannii were detected by conventional methods (2.1% for each).
  6. Mohammed AA, Shantier SW, Mustafa MI, Osman HK, Elmansi HE, Osman IA, et al.
    J Immunol Res, 2020;2020:2567957.
    PMID: 32377531 DOI: 10.1155/2020/2567957
    Background: Nipah belongs to the genus Henipavirus and the Paramyxoviridae family. It is an endemic most commonly found at South Asia and has first emerged in Malaysia in 1998. Bats are found to be the main reservoir for this virus, causing disease in both humans and animals. The last outbreak has occurred in May 2018 in Kerala. It is characterized by high pathogenicity and fatality rates which varies from 40% to 70% depending on the severity of the disease and on the availability of adequate healthcare facilities. Currently, there are no antiviral drugs available for NiV disease and the treatment is just supportive. Clinical presentations for this virus range from asymptomatic infection to fatal encephalitis.

    Objective: This study is aimed at predicting an effective epitope-based vaccine against glycoprotein G of Nipah henipavirus, using immunoinformatics approaches.

    Methods and Materials: Glycoprotein G of the Nipah virus sequence was retrieved from NCBI. Different prediction tools were used to analyze the epitopes, namely, BepiPred-2.0: Sequential B Cell Epitope Predictor for B cell and T cell MHC classes II and I. Then, the proposed peptides were docked using Autodock 4.0 software program. Results and Conclusions. The two peptides TVYHCSAVY and FLIDRINWI have showed a very strong binding affinity to MHC class I and MHC class II alleles. Furthermore, considering the conservancy, the affinity, and the population coverage, the peptide FLIDRINWIT is highly suitable to be utilized to formulate a new vaccine against glycoprotein G of Nipah henipavirus. An in vivo study for the proposed peptides is also highly recommended.

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