Identification of pentadecapeptide mimicking muramyl peptide

Abstract We used monoclonal antibody, generated against N -acetylglucosaminyl-β1-4- N -acetylmuramyl-alanyl- d -isoglutamine (GMDP), and phage display libraries of random peptides to select for oligopeptides, that mimic GMDP in their biological activity. Selected phage clones displayed a peptide RVP...

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Veröffentlicht in:Vaccine 2007-04, Vol.25 (15), p.2900-2906
Hauptverfasser: Laman, Alexander Georgievich, Shepelyakovskaya, Anna Olegovna, Berezin, Igor Anatolevich, Boziev, Khanafi Magometovich, Rodionov, Igor Leonidovich, Chulina, Irina Alexandrovna, Malakhova, Galina Vladimirovna, Brovko, Fedor Alexandrovich, Murashev, Arkadi Nikolaevich, Korpela, Timo Kalevi, Nesmeyanov, Vladimir Andreevich
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Sprache:eng
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Zusammenfassung:Abstract We used monoclonal antibody, generated against N -acetylglucosaminyl-β1-4- N -acetylmuramyl-alanyl- d -isoglutamine (GMDP), and phage display libraries of random peptides to select for oligopeptides, that mimic GMDP in their biological activity. Selected phage clones displayed a peptide RVPPRYHAKISPMVN (called RN-peptide) on their surface. This peptide was synthesized. RN-peptide was shown to augment the antibody response to ovalbumin in mice while the peptide was non-immunogenic and non-pyrogenic. We also characterized adjuvant activity of 14-, 10- and 7-mer analogs of RN-peptide truncated at the C-terminus and found them to be active. Because both carbohydrate and peptide fragments are critical for the biological activity of muramyl peptides, the results indicate that RN-peptide mimicks the spatial structure of intact GMDP.
ISSN:0264-410X
1873-2518
DOI:10.1016/j.vaccine.2006.08.030