Structure-function relationships of tachyplesins and their analogues.

S. Iwanaga, T. Muta, T. Shigenaga, N. Seki, K. Kawano, T. Katsu, Shun-Ichiro Kawabata

Research output: Contribution to journalReview article

37 Citations (Scopus)

Abstract

Haemocytes of the horseshoe crab (Limulus) contain a new family of arthropodous peptide antibiotics, termed the tachyplesin family. These cationic peptides are composed of 17-18 amino acid residues with a C-terminal arginine alpha-amide. Tachyplesin I takes on a fairly rigid conformation constrained by two disulphide bridges and adopts a conformation consisting of an antiparallel beta-sheet connected by a beta-turn. Isopeptides of tachyplesin I with amino acid replacements, tachyplesins II and III, and polyphemusins I and II have also been found in the haemocytes of the South-East Asian species and Limulus polyphemus. These peptides are present in abundance in the small granules of the haemocytes and inhibit strongly the growth of not only Gram-negative and Gram-positive bacteria but also fungi such as Candida albicans. Tachyplesin exists in the prepro form consisting of 77 residues; this precursor is probably processed by intracellular proteases and an amidation enzyme before incorporation into the small granules of the haemocytes. We examined the mode of action of tachyplesin I on biomembranes, comparing it with that of gramicidin S. Tachyplesin caused an efflux of K+ from Staphylococcus aureus and Escherichia coli cells similar to that caused by gramicidin S. Another antimicrobial substance, anti-LPS factor, has been isolated from haemocytes.

Original languageEnglish
JournalCiba Foundation symposium
Volume186
Publication statusPublished - Jan 1 1994

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Hemocytes
Horseshoe Crabs
Gramicidin
Peptides
Amino Acids
Tachypleus tridentatus tachyplesin peptide
Gram-Positive Bacteria
Candida albicans
Amides
Disulfides
Arginine
Staphylococcus aureus
Peptide Hydrolases
Fungi
Escherichia coli
Anti-Bacterial Agents
Enzymes
Growth

All Science Journal Classification (ASJC) codes

  • General

Cite this

Iwanaga, S., Muta, T., Shigenaga, T., Seki, N., Kawano, K., Katsu, T., & Kawabata, S-I. (1994). Structure-function relationships of tachyplesins and their analogues. Ciba Foundation symposium, 186.

Structure-function relationships of tachyplesins and their analogues. / Iwanaga, S.; Muta, T.; Shigenaga, T.; Seki, N.; Kawano, K.; Katsu, T.; Kawabata, Shun-Ichiro.

In: Ciba Foundation symposium, Vol. 186, 01.01.1994.

Research output: Contribution to journalReview article

Iwanaga, S, Muta, T, Shigenaga, T, Seki, N, Kawano, K, Katsu, T & Kawabata, S-I 1994, 'Structure-function relationships of tachyplesins and their analogues.', Ciba Foundation symposium, vol. 186.
Iwanaga S, Muta T, Shigenaga T, Seki N, Kawano K, Katsu T et al. Structure-function relationships of tachyplesins and their analogues. Ciba Foundation symposium. 1994 Jan 1;186.
Iwanaga, S. ; Muta, T. ; Shigenaga, T. ; Seki, N. ; Kawano, K. ; Katsu, T. ; Kawabata, Shun-Ichiro. / Structure-function relationships of tachyplesins and their analogues. In: Ciba Foundation symposium. 1994 ; Vol. 186.
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