Bio

Bio


I am a respiratory/immunology research scientist specialized in asthma, idiopathic pulmonary fibrosis, pulmonary hypertension, chronic obstructive pulmonary disease and respiratory infectious disease. My academic and research training across 4 nations and 3 continents has given me skills in immunology, microbiology, molecular biology, cell biology and metal biology techniques. Currently, I am working as a postdoctoral research fellow on targeting novel BMPR2 modifiers in pulmonary aertial hypertension with repurposed drugs at the division of pulmonary and critical care medicine, Stanford University, USA. My longer-term goal is to discover novel drug for unmet medical needs in critical respiratory diseases.

Honors & Awards


  • PhD Award, The University of Newcastle, Australia (2018)
  • Travel Award, The Thoracic Society of Australia and New Zealand (TSANZ) Travel Award (2017)
  • Postgraduate Research Scholarship, The University of Newcastle, Australia (2014)
  • MS Award, Chung-Ang University, South Korea (2013)
  • Young Scientist Award, Chung-Ang University Young Scientist Award (CAYSS) (2011)
  • B.Sc Honors Award, Khulna University, Bangladesh (2009)
  • Merit Scholarship Award, Khulna University, Bangladesh (2008)

Boards, Advisory Committees, Professional Organizations


  • Member, World Association for Bronchology and Interventional Pulmonology (2018 - Present)
  • Member, European Respiratory Society (2017 - Present)
  • Member, The Thoracic Society for Australia and New Zealand (2016 - Present)
  • Member, International BioIron Society (2015 - Present)
  • Member, International society for infectious diseases (2015 - Present)
  • Member, Asia Pacific Association of Pediatric Allergy, Respirology and Immunology (2015 - Present)
  • Member, Priority Research Centre-Healthy Lungs, University of Newcastle, Australia (2014 - Present)

Professional Education


  • Master of Science, Unlisted School (2013)
  • Doctor of Philosophy, University Of Newcastle (2018)
  • Bachelor of Science, Unlisted School (2010)

Stanford Advisors


Publications

All Publications


  • Impaired induction of Slc26a4 promotes respiratory acidosis and severe, steroid-resistant asthma Kim, R., Pinkerton, J. W., Rae, B. E., Mayall, J. R., Brown, A. C., Nli, M., Goggins, B. J., Essilfie, A., Starkey, M. R., To, C., Bosco, A., Horvat, J. C., Hansbro, P. M. AMER ASSOC IMMUNOLOGISTS. 2017
  • HIGH FAT DIET-INDUCED OBESITY PROMOTES STEROID-RESISTANT ASTHMA THROUGH AN NLRP3 INFLAMMASOME-DEPENDENT MECHANISM Pinkerton, J., Kim, R., Mayall, J., Ali, M., Starkey, M., Robertson, A., O'Neill, L., Cooper, M., Hansbro, P., Horvat, J. WILEY. 2017: 65
  • IMPAIRED INDUCTION OF SLC26A4 PROMOTES RESPIRATORY ACIDOSIS AND SEVERE, STEROID-INSENSITIVE ASTHMA Horvat, J., Pinkerton, J., Rae, B., Mayall, J., Brown, A., Ali, M., Goggins, B., Essilfie, A., Starkey, M., Bosco, A., Kim, R., Hansbro, P. WILEY. 2017: 65
  • Role of iron in the pathogenesis of respiratory disease. The international journal of biochemistry & cell biology Ali, M. K., Kim, R. Y., Karim, R., Mayall, J. R., Martin, K. L., Shahandeh, A., Abbasian, F., Starkey, M. R., Loustaud-Ratti, V., Johnstone, D., Milward, E. A., Hansbro, P. M., Horvat, J. C. 2017; 88: 181–95

    Abstract

    Iron is essential for many biological processes, however, too much or too little iron can result in a wide variety of pathological consequences, depending on the organ system, tissue or cell type affected. In order to reduce pathogenesis, iron levels are tightly controlled in throughout the body by regulatory systems that control iron absorption, systemic transport and cellular uptake and storage. Altered iron levels and/or dysregulated homeostasis have been associated with several lung diseases, including chronic obstructive pulmonary disease, lung cancer, cystic fibrosis, idiopathic pulmonary fibrosis and asthma. However, the mechanisms that underpin these associations and whether iron plays a key role in the pathogenesis of lung disease are yet to be fully elucidated. Furthermore, in order to survive and replicate, pathogenic micro-organisms have evolved strategies to source host iron, including freeing iron from cells and proteins that store and transport iron. To counter these microbial strategies, mammals have evolved immune-mediated defence mechanisms that reduce iron availability to pathogens. This interplay between iron, infection and immunity has important ramifications for the pathogenesis and management of human respiratory infections and diseases. An increased understanding of the role that iron plays in the pathogenesis of lung disease and respiratory infections may help inform novel therapeutic strategies. Here we review the clinical and experimental evidence that highlights the potential importance of iron in respiratory diseases and infections.

    View details for DOI 10.1016/j.biocel.2017.05.003

    View details for PubMedID 28495571

  • Impaired Induction Of Slc26a4 Promotes Respiratory Acidosis And Severe, Steroid-Insensitive Asthma Kim, R. Y., Pinkerton, J. W., Rae, B., Mayall, J. R., Brown, A. C., Ali, M., Goggins, B., Essilfie, A., Starkey, M. R., Bosco, A., Horvat, J. C., Hansbro, P. M. AMER THORACIC SOC. 2017
  • Role Of Increased Iron Levels In The Pathogenesis Of Lung Disease Horvat, J. C., Alit, M., Johnstone, D., Essilfie, A., Mayall, J., Pinkerton, J. W., Donovan, C., Liu, G., Martina, K., Milward, A. E., Hansbro, P. M. AMER THORACIC SOC. 2017
  • Role for NLRP3 Inflammasome-mediated, IL-1β-Dependent Responses in Severe, Steroid-Resistant Asthma. American journal of respiratory and critical care medicine Kim, R. Y., Pinkerton, J. W., Essilfie, A. T., Robertson, A. A., Baines, K. J., Brown, A. C., Mayall, J. R., Ali, M. K., Starkey, M. R., Hansbro, N. G., Hirota, J. A., Wood, L. G., Simpson, J. L., Knight, D. A., Wark, P. A., Gibson, P. G., O'Neill, L. A., Cooper, M. A., Horvat, J. C., Hansbro, P. M. 2017; 196 (3): 283–97

    Abstract

    Severe, steroid-resistant asthma is the major unmet need in asthma therapy. Disease heterogeneity and poor understanding of pathogenic mechanisms hampers the identification of therapeutic targets. Excessive nucleotide-binding oligomerization domain-like receptor family, pyrin domain-containing 3 (NLRP3) inflammasome and concomitant IL-1β responses occur in chronic obstructive pulmonary disease, respiratory infections, and neutrophilic asthma. However, the direct contributions to pathogenesis, mechanisms involved, and potential for therapeutic targeting remain poorly understood, and are unknown in severe, steroid-resistant asthma.To investigate the roles and therapeutic targeting of the NLRP3 inflammasome and IL-1β in severe, steroid-resistant asthma.We developed mouse models of Chlamydia and Haemophilus respiratory infection-mediated, ovalbumin-induced severe, steroid-resistant allergic airway disease. These models share the hallmark features of human disease, including elevated airway neutrophils, and NLRP3 inflammasome and IL-1β responses. The roles and potential for targeting of NLRP3 inflammasome, caspase-1, and IL-1β responses in experimental severe, steroid-resistant asthma were examined using a highly selective NLRP3 inhibitor, MCC950; the specific caspase-1 inhibitor Ac-YVAD-cho; and neutralizing anti-IL-1β antibody. Roles for IL-1β-induced neutrophilic inflammation were examined using IL-1β and anti-Ly6G.Chlamydia and Haemophilus infections increase NLRP3, caspase-1, IL-1β responses that drive steroid-resistant neutrophilic inflammation and airway hyperresponsiveness. Neutrophilic airway inflammation, disease severity, and steroid resistance in human asthma correlate with NLRP3 and IL-1β expression. Treatment with anti-IL-1β, Ac-YVAD-cho, and MCC950 suppressed IL-1β responses and the important steroid-resistant features of disease in mice, whereas IL-1β administration recapitulated these features. Neutrophil depletion suppressed IL-1β-induced steroid-resistant airway hyperresponsiveness.NLRP3 inflammasome responses drive experimental severe, steroid-resistant asthma and are potential therapeutic targets in this disease.

    View details for DOI 10.1164/rccm.201609-1830OC

    View details for PubMedID 28252317

  • Investigating antioxidant therapy for steroid-resistant asthma Pinkerton, J., Kim, R., Essilfie, A., Rae, B., Mayall, J., Ali, M., Starkey, M., Wood, L., Biswal, S., Horvat, J., Hansbro, P. EUROPEAN RESPIRATORY SOC JOURNALS LTD. 2016
  • TARGETING OXIDATIVE STRESS FOR THE SUPPRESSION OF SEVERE, STEROID-INSENSITIVE ASTHMA Pinkerton, J., Kim, R., Essilfie, A., Rae, B., Mayall, J., Ali, M., Starkey, M., Wood, L., Biswal, S., Horvat, J., Hansbro, P. WILEY-BLACKWELL. 2016: 105
  • Knockdown of the host cellular protein transportin 3 attenuates prototype foamy virus infection BIOSCIENCE BIOTECHNOLOGY AND BIOCHEMISTRY Ali, M., Kim, J., Hamid, F., Shin, C. 2015; 79 (6): 943–51

    Abstract

    Transportin 3 (TNPO3) is a member of the importin-ß superfamily proteins. Despite numerous studies, the exact molecular mechanism of TNPO3 in retroviral infection is still controversial. Here, we provide evidence for the role and mechanism of TNPO3 in the replication of prototype foamy virus (PFV). Our findings revealed that PFV infection was reduced 2-fold by knockdown (KD) of TNPO3. However, late stage of viral replication including transcription, translation, viral assembly, and release was not influenced. The differential cellular localization of PFV integrase (IN) in KD cells pinpointed a remarkable reduction of viral replication at the nuclear import step. We also found that TNPO3 interacted with PFV IN but not with Gag, suggesting that IN-TNPO3 interaction is important for nuclear import of PFV pre-integration complex. Our report enlightens the mechanism of PFV interaction with TNPO3 and support ongoing research on PFV as a promising safe vector for gene therapy.

    View details for DOI 10.1080/09168451.2015.1008973

    View details for Web of Science ID 000356239400011

    View details for PubMedID 25660973

  • Nuclear localization signals in prototype foamy viral integrase for successive infection and replication in dividing cells. Molecules and cells Hossain, A., Ali, K., Shin, C. G. 2014; 37 (2): 140–48

    Abstract

    We identified four basic amino acid residues as nuclear localization signals (NLS) in the C-terminal domain of the prototype foamy viral (PFV) integrase (IN) protein that were essential for viral replication. We constructed seven point mutants in the C-terminal domain by changing the lysine and arginine at residues 305, 308, 313, 315, 318, 324, and 329 to threonine or proline, respectively, to identify residues conferring NLS activity. Our results showed that mutation of these residues had no effect on expression assembly, release of viral particles, or in vitro recombinant IN enzymatic activity. However, mutations at residues 305 (R → T), 313(R → T), 315(R → P), and 329(R → T) lead to the production of defective viral particles with loss of infectivity, whereas non-defective mutations at residues 308(R → T), 318(K → T), and 324(K → T) did not show any adverse effects on subsequent production or release of viral particles. Sub-cellular fractionation and immunostaining for viral protein PFV-IN and PFV-Gag localization revealed predominant cytoplasmic localization of PFV-IN in defective mutants, whereas cytoplasmic and nuclear localization of PFV-IN was observed in wild type and non-defective mutants. However sub-cellular localization of PFV-Gag resulted in predominant nuclear localization and less presence in the cytoplasm of the wild type and non-defective mutants. But defective mutants showed only nuclear localization of Gag. Therefore, we postulate that four basic arginine residues at 305, 313, 315 and 329 confer the karyoplilic properties of PFV-IN and are essential for successful viral integration and replication.

    View details for DOI 10.14348/molcells.2014.2331

    View details for PubMedID 24598999

    View details for PubMedCentralID PMC3935627

  • Comparative sequence and expression analyses of African green monkey (Cercopithecus aethiops) TNPO3 from CV-1 cells GENES & GENOMICS Ali, M., Hossain, M., Shin, C. 2013; 35 (4): 549–58
  • Structural and Functional Insights into Foamy Viral Integrase VIRUSES-BASEL Hossain, M., Ali, M., Shin, C. 2013; 5 (7): 1850–66

    Abstract

    Successful integration of retroviral DNA into the host chromosome is an essential step for viral replication. The process is mediated by virally encoded integrase (IN) and orchestrated by 3'-end processing and the strand transfer reaction. In vitro reaction conditions, such as substrate specificity, cofactor usage, and cellular binding partners for such reactions by the three distinct domains of prototype foamy viral integrase (PFV-IN) have been described well in several reports. Recent studies on the three-dimensional structure of the interacting complexes between PFV-IN and DNA, cofactors, binding partners, or inhibitors have explored the mechanistic details of such interactions and shown its utilization as an important target to develop anti-retroviral drugs. The presence of a potent, non-transferable nuclear localization signal in the PFV C-terminal domain extends its use as a model for investigating cellular trafficking of large molecular complexes through the nuclear pore complex and also to identify novel cellular targets for such trafficking. This review focuses on recent advancements in the structural analysis and in vitro functional aspects of PFV-IN.

    View details for DOI 10.3390/v5071850

    View details for Web of Science ID 000322172200016

    View details for PubMedID 23872492

    View details for PubMedCentralID PMC3738965