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Curriculum Vitae

Provide a brief CV showing education and research training, including any prizes or

awards: (no more than one page)

Mohammad Riazul Islam, PhD

Assistant Professor, Dept. of Biochemistry and Molecular Biology, Faculty of

Biological Science, University of Dhaka, Dhaka-1000, Bangladesh

Tel: (0880)-2-9661900 ext. 7663 E-mail: riazul_i@yahoo.com

Date of Birth: 22 October, 1976

Education:

2006-2009: PhD in Bioscience and Biotechnology, Kyushu University, Japan.

2004-2005: Post Graduate training in Biotechnology, Osaka University,

Japan

1998-1999: Master of Science in Biochemistry, University of Dhaka,

Bangladesh

1996-1998: Bachelor of Science in Biochemistry, University of Dhaka,

Bangladesh

Employment:

July 2012 – Till now

Assistant Professor, Department of Biochemistry and Molecular Biology,

University of Dhaka, Bangladesh

July 2010- June 2012

JSPS Post-doctoral Research Fellow, Laboratory of Microbial Technology,

Faculty of Agriculture, Kyushu University, Japan

October 2009- June 2010

Assistant Professor, Department of Biochemistry and Molecular Biology,

University of Dhaka, Bangladesh

April 2004 - September 2004

Lecturer, Department of Biochemistry and Molecular Biology, University of

Dhaka, Bangladesh

July 2002 – April 2004:

Research Officer, Tuberculosis Laboratory, International Center for Diarrheal Disease

Research, Bangladesh (ICDDR’B)

Awards and Fellowships:

Japan Society for Promotion of Science (JSPS) post-doctoral fellowship (2010-2012)

Distinction of Young Scientist in ‘Second International Symposium on Antimicrobial

Peptide, Saint-Malo, France’, June 2009

‘MONBUKAGAHUSHO (MEXT, Japan) scholarship’ for completion of PhD in

Kyushu University, Japan, 2006-2009

‘UNESCO Post Graduate Inter-University Course in Biotechnology, 2004’

fellowship, ICBiotech, Osaka University, Japan, 2004-2005.

Professional Memberships:

Japan Society for Bioscience, Biotechnology, and Agrochemistry

(JSBBA)

American Chemical Society (ACS)

Bangladesh Society for Biochemistry and Molecular Biology (BSBMB)

Graduate Biochemist Association (GBA)

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List of Publications in International Journals*

* Number all publications in international journals or book chapters, with earliest first and

most recent at the end. Provide the Impact Factor (IF) of the journal and indicate your

contribution the work described and the publication. Use as many pages as required. Follow

the style in these examples:

1. S. Banu , S. V. Gordon, S. Palmer, M. R. Islam, S. Ahmed , K. M. Alam, S. T. Cole, R.

Brosch. Genotypic analysis of Mycobacterium tuberculosis in Bangladesh and prevalence

of the Beijing strain. Journal of Clinical Microbiology 42, 674-82 (2004) (IF 4.15)

In this article, MRI’s contribution was in performing the experiments of deletion analysis

and MIRU-VNTR analysis for genotyping.

2. M. R. Islam, J. Nagao, K. Shioya, J. Nakayama, K. Sonomoto. Characterization of

nukacin ISK-1 biosynthetic enzymes by expressing nukacin ISK-1-lacticin 481 chimeric

prepeptides. Annual Report ICBiotech, Osaka University 27, 801-811(2005)

In this article, MRI contributed in all parts.

3. J. Nagao, Y. Morinaga, M. R. Islam, S. M. Asaduzzaman, Y. Aso, J. Nakayama, K.

Sonomoto. Mapping and identification of the region and secondary structure required for

the maturation of the nukacin ISK-1 prepeptide. Peptides 30, 1412-1420 (2009) (IF 2.43)

In this article, MRI’s contribution was to construction of chimera peptide and their

characterization.

4. M. R. Islam, K. Shioya, J. Nagao, M. Nishie, H. Jikuya, T. Zendo, J. Nakayama, K.

Sonomoto. Evaluation of essential and variable residues of nukacin ISK-1 by NNK

scanning. Molecular Microbiology l72, 1438–1447 (2009) (IF 5.01)

Most of the work in this article was done by MRI.

5. S. Banu, M. K. M. Uddin, M. R. Islam, K. Zaman, T. Ahmed, A. H. Talukder, M. T.

Rahman, Z. Rahim, N. Akter, N. Khatun, R. Brosch, H. P. Endtz. Molecular

epidemiology of tuberculosis in rural matlab, Bangladesh. International Journal of

Tuberculosis and Lung Disease 16, 319-326 (2012) (IF 2.73)

In this article MIRU-VNTR and spoligotyping experiments was done by MRI.

6. T. V. Puramattathu, M. R. Islam, M. Nishie, S. Yanagihara, J. Nagao, K. Okuda, T.

Zendo, J. Nakayama, K. Sonomoto. Enhanced production of nukacin D13E in

Lactococcus lactis NZ9000 by the additional expression of immunity genes. Applied

Microbiology and Biotechnology 93, 671-678 (2012) (IF 3.42)

In this article the D13E mutant was constructed by MRI and overall supervision of this

work was also done by him.

7. M. R. Islam, M. Nishie, J. Nagao, T. Zendo, S. Keller, J. Nakayama, D. Kohda, H-G.

Sahl, K. Sonomoto. Ring A of Nukacin ISK-1: A Lipid II-Binding Motif for Type-A(II)

Lantibiotic. Journal of American Chemical Society 134, 3687-90 (2012) (IF 9.9)

In this article, MRI contributed in most of the parts, as generation of ring A variants,

peptidoglycan precursor accumulation experiment and interaction analysis.

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Abstract

Indicate below the abstract that is submitted by you for presentation at the YSP and the

FAOBMB Congress in Bangkok (include all authors, affiliation(s) and the text of the

abstract)

Title: Ring A of nukacin ISK-1: a lipid II-binding motif for type-A(II) lantibiotic

Mohammad R. Islam1, Mami Nishie

1, Jun-ichi Nagao

2,

Takeshi Zendo1, Jiro

Nakayama1, Daisuke Kohda

3, Hans-Georg Sahl

4 and Kenji Sonomoto

1

1Laboratory of Microbial Technology, Faculty of Agriculture, Kyushu University,

Japan; 2Section of Infection Biology, Fukuoka Dental College, Japan;

3Division of

Structural Biology, Medical Institute of Bio-regulation, Kyushu University, Japan; 4Institute of Medical Microbiology, University of Bonn, Germany

E-mail: riazul_i@yahoo.com

Nukacin ISK-1 is a type-A(II) lantibiotic consisting of 27 amino acids with a linear N-

terminal and globular C-terminal region (1). The ring A of nukacin ISK-1, which is

also present in different type-A(II) lantibiotics, resembles a lipid II-binding motif

(TxS/TxD/EC, x denotes undefined residues) similar to that present in mersacidin

(type-B lantibiotics), which suggests that nukacin ISK-1 binds to lipid II as a docking

molecule. Results from our experiments on peptidoglycan precursor (UDP-MurNAc-

pp) accumulation and peptide antagonism assays clearly indicated that nukacin ISK-1

inhibits cell wall biosynthesis accumulating lipid II precursor inside the cell and the

peptide activity can be repressed by lipid I and lipid II. Interaction analysis of nukacin

ISK-1 and different ring A variants with lipid II revealed that nukacin ISK-1 and

nukacin D13E (a more active variant) have a high affinity (KD, 0.17 µM and 0.19 µM

respectively) for lipid II, whereas, nukacin D13A (a less active variant) showed a

lower affinity and nukacin C14S (a negative variant lacking the ring A structure)

exhibited no interaction. Therefore on the basis of the structural similarity and

positional significance of the amino acids in this region, we concluded that nukacin

ISK-1 binds lipid II via its ring A region, and may lead to the inhibition of cell-wall

biosynthesis (2).

Keywords: lantibiotics, nukacin ISK-1, lipid II-binding motif

References

1. Asaduzzaman, S. M., Sonomoto, K. (2009) Lantibiotics: diverse activities and

unique modes of action. J. Biosci. Bioeng. 107, 475-487

2. Islam, M. R., Nishie, M., Nagao, J., Zendo, T., Keller, S., Nakayama, J., Kohda, D.,

Sahl, H-G., Sonomoto, K. (2012) Ring A of nukacin ISK-1: a lipid II-binding motif

for type-A(II) lantibiotic. J. Am. Chem. Soc. 134, 3687-3690

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Personal Statement

Indicate briefly here your Research Interests and Career Goals, why you are interested

to participate in the YSP Program (including what you will bring to the YSP and what

you hope to gain from it): (no more than one page)

After completion of my post-doctoral fellowship from Japan in June 2012, I started working

in the Dept. of Biochemistry and Molecular Biology, University of Dhaka, Bangladesh, as an

Assistant Professor. In Japan, during my PhD and post-doctoral fellowship, I carried out

research on antimicrobial peptide bioengineering and elucidation of their mode of action. I

used a model peptide nukacin ISK-1, a ribosomally synthesized and lanthionine containing

antimicrobial peptide produced by Gram-positive bacteria and having 27 amino acid residues,

for bioengineering to create higher potential peptide variants and to identify the docking

molecule for its antimicrobial mechanism. I used site saturation systematic mutagenesis for

lantibiotic bioengineering and obtained two high potential peptide variants, that has been

published in Molecular Microbiology journal in 2009. I also identified the docking molecule

of nukacin ISK-1 as lipid II, during its antimicrobial mechanism and the binding motif of

nukacin ISK-1 required for lipid II interaction. We also published this work in Journal of

American Chemical Society (JACS) in 2012. Now in Bangladesh, I would like to focus the

following things and would like to continue my research in the same field.

Screening of potential antimicrobial peptide from the natural sources:

Due to the emergence of drug resistant pathogens, it is now inevitable to find out alternative

therapeutic agents apart from the conventional antibiotics. In that case, antimicrobial peptides

are the promising candidates because of their higher potency and suitable to change the

structure by mutagenesis. Therefore, we are planning to search for potential antimicrobial

candidate from the nature such as soil, water, plants etc. We will use the conventional

procedure for the initial screening.

Generation of high potential peptide variants by bioengineering:

Using molecular biology technique, we will identify the biosynthetic mechanism of identified

peptide. To generate high potential peptide variants, we will perform structure-function study

in depth.

Elucidation of their antimicrobial mechanism:

To identify the antimicrobial mechanism we will investigate the membrane interaction,

searching for docking molecule and identification of the binding motif of peptide.

Investigation of molecular mechanism for As/Pb metabolism by soil isolated bacteria for

As/Pb removal:

Arsenic (As) problem in Bangladesh is very critical. This contamination is no longer been in

drinking water only; rather it is now speeding in the food chain. We need to find out

alternative methods to mitigate this As contamination such as, using microorganisms.

Microbes are mostly convenient as they can be easily manipulated. We identified few strains

from the As contaminated area and found their higher efficiency for As removal. We will now

investigate their mechanism of As metabolism and their use for As removal.

Lead (Pb) contamination is also a vital problem in Bangladesh. Most of the industrial areas

are heavily contaminated by Pb. Therefore to remove Pb from surface water and soil, we are

planning to use microbes that can degrade Pb. We will screen such microbes form the natural

sources and will try to investigate the mechanism for Pb degradation.

Through joining this congress I can make a good communication with the leading scientists

and would like to make some collaboration for my research. I strongly believe that this

congress can be a good platform to discuss my current and future research proposals.

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Attachments:

Recommendation letter 1

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Recommendation letter 2