Identification of an antimicrobial peptide from large freshwater snail (Lymnaea stagnalis): activity against antibiotics resistant Staphylococcus epidermidis

Samiran Sona Gauri; Chandan Kumar Bera; Rabindranath Bhattacharyya; Santi Mohan Mandal

doi:10.52756/ijerr.2016.v2.002

Authors

Samiran Sona Gauri Central Research Facility, Indian Institute of Technology Kharagpur, 721302, WB, India
Chandan Kumar Bera Central Research Facility, Indian Institute of Technology Kharagpur, 721302, WB, India
Rabindranath Bhattacharyya Department of Botany, Presidency College, Kolkata – 700 073 West Bengal, India
Santi Mohan Mandal Central Research Facility, Indian Institute of Technology Kharagpur, 721302, WB, India

DOI:

https://doi.org/10.52756/ijerr.2016.v2.002

Keywords:

Antibiotic resistant, antimicrobial peptides, L. stagnalis, S. epidermidis

Abstract

Nowadays, antibiotic resistance in bacteria is a great public health problem of increasing magnitude due to quick evolution through mutation that has generated the urgency to find the effective solutions to address this problem. Aside the conventional antibiotics, antimicrobial peptides are a new class of antimicrobials is known to have the activity against a wide range of bacteria. An antimicrobial peptide was isolated and purified from the Lymnaea stagnalis, a fresh water large snail, using ultrafiltration and reversed phase liquid chromatography. The molecular mass of the peptide 2345 Da was determined using MALDI TOF mass spectrometry. This peptide is efficiently prevented the growth of Staphylococcus epidermidis that resistant to ampicillin and chloramphenicol antibiotics. The MIC value was 16 ?g/mL and specifically damage to bacterial membranes. Hence, this reported peptide revealed an alternative candidate to controlling the Staphylococcal infections.

References

Gauri, S. S., Mandal, S. M., Pati, B. R. and Dey, S. (2011). Purification and structural characterization of a novel antibacterial peptide from Bellamya bengalensis: Activity against ampicillin and chloramphenicol resistant Staphylococcus epidermidis. Peptides. 32: 691-696.

Jack, R. W., Tagg, J. R. and Ray, B. (1995). Bacteriocins of gram-positive bacteria. Microbiol. Rev. 59: 171-200.

Larrick, J. W. and Wright, S. C. (1996). Cationic antimicrobial peptides. Drugs Future. 21: 41-48.

Lehrer, R. I., Lichtenstein, A. K. and Ganz, T. (1993). Defensins: antimicrobial and cytotoxic peptides of mammalian cells. Annu. Rev. Immunol. 11: 105-128.

Lorenzini, D. M., Da Silva, P. I., Fogaca, A. C., Bulet, P. and Daffre, S. (2003). Acanthoscurrin: a novel glycine-rich antimicrobial peptide constitutively expressed in the hemocytes of the spider Acanthoscurria gomesiana. Dev. Comp. Immunol. 27:781-791.

Mandal, S. M., Dey, S., Mandal, M., Sarkar, S., Maria-Neto, S. and Franco, O. L. (2009). Identification and structural insights of three novel antimicrobial peptides isolated from green coconut water. Peptides. 30: 633–637.

Olivera, B. M., Ramachandran, J., Miljanich, G. and Adams, M. E. (1994). Calcium channel diversity and neurotransmitter release: The -conotoxins and the ωagatoxins. Annu. Rev. Biochem. 63: 823- 867.

Olivera, B. M., Rivier, J., Clark, C., Ramilo, C. A., Corpuz, G. P., Abogadie, F. C., Mena, E. E., Woodward, S. R., Hillyard, D. R. and Cruz, L. J. (1990). Diversity of Conus neuropeptides. Science. 249: 257–263.

Schoenbaum, S. C., Gardner, P. and Shillito, J. (1975). Infection of cerebrospinal fluid shunts: epidemiology, clinical manifestations and therapy. J. Infect. Dis.131: 543-552.

Zelezetsky, I., Pag, U., Sahl, H. G. and Tossi, A. (2005). Tuning the biological properties of amphipathic alpha-helical antimicrobial peptides: rational use of minimal amino acid substitutions. Peptides. 26: 2368–2376.