* To whom correspondence should be addressed.
Received February 16, 2006; Revision received July 18, 2006
An approach for isolation of an autoagglutination factor (AF) from Hms- cells of the plague agent has been developed. Purified AF has been obtained and characterized in physicochemical properties. The AF is found to be a complex of a 17.5-kD protein with a low molecular weight peptide component, which binds iron ions and shows siderophore activity. This low molecular weight component is responsible for hydrophobic properties and immunochemical activity of the AF, as well as for its ability to interact with the plague diagnosticum L-413c bacteriophage.
KEY WORDS: plague agent Yersinia pestis, Hms- cells, autoagglutination factorDOI: 10.1134/S0006297906110046