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PMID:1717472

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Citation

Moore, KS, Bevins, CL, Brasseur, MM, Tomassini, N, Turner, K, Eck, H and Zasloff, M (1991) Antimicrobial peptides in the stomach of Xenopus laevis. J. Biol. Chem. 266:19851-7

Abstract

Antimicrobial peptides are widely distributed in nature and appear to play a role in the host defense of plants and animals. In this study we report the existence of antimicrobial peptides in the stomach of the vertebrate Xenopus laevis, an animal previously shown to store high concentrations of antimicrobial peptides in its skin. Antimicrobial activity was detected in extracts of X. laevis stomach tissue and nine antimicrobial peptides were then purified. A novel 24-amino acid peptide, designated PGQ, was isolated from these extracts, and has the following amino acid sequence: GVLSNVIGYLKKLGTGALNAVLKQ. PGQ is relatively basic and has the potential to form an amphipathic alpha-helix. The other peptides isolated are members of the magainin family of antimicrobial peptides, and include magainins I and II, PGLa, xenopsin precursor fragment, and four caerulein precursor fragments. None of these peptides had been previously identified in tissues other than the skin. The purification of the peptides from stomach extracts and subsequent protein sequence analysis reveals that the peptides have undergone the same processing as their dermal counterparts, and that they are stored in their processed forms. Northern blot analysis indicates that the magainin family of peptides are synthesized in the stomach, and immunohistochemical studies demonstrate that magainin is stored in a novel granular multinucleated cell in the gastric mucosa of Xenopus. This study demonstrates that the magainin family of antimicrobial peptides is found in the gastrointestinal system of X. laevis and offers an opportunity to further define the physiological role of these defense peptides.

Links

PubMed

Keywords

Amino Acid Sequence; Animals; Anti-Infective Agents/isolation & purification; Blotting, Northern; Chromatography, High Pressure Liquid; Electrophoresis; Molecular Sequence Data; Peptides/pharmacology; RNA/analysis; Skin/chemistry; Stomach/chemistry; Xenopus laevis

Significance

Annotations

Gene product Qualifier GO Term Evidence Code with/from Aspect Extension Notes Status

XENLA:PYLAA

GO:0002775: antimicrobial peptide production

ECO:0000314:

P

Fig 3; according to Table 1, pglA has a reversed-phase HPLC fraction of 57. When plated on a lawn of E. coli, the area where the product of pglA was plated (#57) shows a significant amount of lysis of the surrounding bacteria.

complete
CACAO 4910


See also

References

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