Difference between revisions of "Part:BBa K1162007"
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An antimicrobial peptide from the cathelicidin family of peptides, isolated from the tammar wallaby (<i>Macropus eugenii</i>). WAM-1 is one of several identified peptides that are produced in the mammary gland throughout lactation in order to supply protection from infection to the young wallabies that have underdeveloped immune systems. This is evident through the down-regulation of these peptides in the tammar wallaby milk at around 100 days after birth, the same period that the wallaby young develop immunocompetence (Wang, et. al 2011). | An antimicrobial peptide from the cathelicidin family of peptides, isolated from the tammar wallaby (<i>Macropus eugenii</i>). WAM-1 is one of several identified peptides that are produced in the mammary gland throughout lactation in order to supply protection from infection to the young wallabies that have underdeveloped immune systems. This is evident through the down-regulation of these peptides in the tammar wallaby milk at around 100 days after birth, the same period that the wallaby young develop immunocompetence (Wang, et. al 2011). | ||
− | Similar to other members of the cathelicidin family, the WAM-1 antimicrobial peptide has been shown to be effective against a broad range of bacterial pathogens (Kastin, A. J. 2013). Specifically, a group of researchers from Australia (Wang, et. al 2011) have tested this peptide, isolated from its natural source, against several gram-negative (<i>E. coli</i>, <i>P. aeruginosa</i>, among others) and gram-positive (<i>B. subtilis</i>, <i>S. aureus</i>, among others) bacterium with minimum inhibitory concentration (MIC) values that indicate highly effective antibiotic activity. To our knowledge, this antimicrobial peptide has not been expressed | + | Similar to other members of the cathelicidin family, the WAM-1 antimicrobial peptide has been shown to be effective against a broad range of bacterial pathogens (Kastin, A. J. 2013). Specifically, a group of researchers from Australia (Wang, et. al 2011) have tested this peptide, isolated from its natural source, against several gram-negative (<i>E. coli</i>, <i>P. aeruginosa</i>, among others) and gram-positive (<i>B. subtilis</i>, <i>S. aureus</i>, among others) bacterium with minimum inhibitory concentration (MIC) values that indicate highly effective antibiotic activity. To our knowledge, this antimicrobial peptide has not been previously expressed or purified recombinantly in <i>E. coli</i>. |
===References:=== | ===References:=== |
Latest revision as of 02:20, 26 September 2013
WAM-1 antimicrobial peptide from the tammar wallaby (Macropus eugenii)
An antimicrobial peptide from the cathelicidin family of peptides, isolated from the tammar wallaby (Macropus eugenii). WAM-1 is one of several identified peptides that are produced in the mammary gland throughout lactation in order to supply protection from infection to the young wallabies that have underdeveloped immune systems. This is evident through the down-regulation of these peptides in the tammar wallaby milk at around 100 days after birth, the same period that the wallaby young develop immunocompetence (Wang, et. al 2011).
Similar to other members of the cathelicidin family, the WAM-1 antimicrobial peptide has been shown to be effective against a broad range of bacterial pathogens (Kastin, A. J. 2013). Specifically, a group of researchers from Australia (Wang, et. al 2011) have tested this peptide, isolated from its natural source, against several gram-negative (E. coli, P. aeruginosa, among others) and gram-positive (B. subtilis, S. aureus, among others) bacterium with minimum inhibitory concentration (MIC) values that indicate highly effective antibiotic activity. To our knowledge, this antimicrobial peptide has not been previously expressed or purified recombinantly in E. coli.
References:
Wang, J.; Wong, E. S. W.; Whitley, J. C.; Li, J.; Stringer, J. M.; Short, K. R.; Renfree, M. B.; Belov, K.; Cocks, B. G., Ancient Antimicrobial Peptides Kill Antibiotic-Resistant Pathogens: Australian Mammals Provide New Options. PLoS ONE 2011, 6 (8).
Kastin, A. J., Handbook of Biologically Active Peptides (Second Edition). Chapter 15: Cathelicidins, p. 77-84.
Sequence and Features
- 10COMPATIBLE WITH RFC[10]
- 12COMPATIBLE WITH RFC[12]
- 21COMPATIBLE WITH RFC[21]
- 23COMPATIBLE WITH RFC[23]
- 25COMPATIBLE WITH RFC[25]
- 1000COMPATIBLE WITH RFC[1000]