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Cover photograph (Copyright © 2009, American Society for Microbiology. All Rights Reserved.): Interaction of Mycoplasma penetrans ADP-ribosylating and vacuolating cytotoxin MYPE9110 with human cells. HeLa cell monolayers were intoxicated with full-length recombinant MYPE9110 (rMYPE9110; amino acids 1–591) and incubated for 1 h. Cells were fixed, and MYPE9110 was visualized using AlexaFluor 633-coupled antibodies (red). Cells were counterstained with 4′,6-diamidino-2-phenylindole (DAPI [blue]) and AlexaFluor 488 (phalloidin [green]). As depicted, immunofluorescence microscopy revealed binding and internalization of full-length rMYPE9110. In contrast, truncated rMYPE9110 (amino acids 1–300), which retains the amino-terminal region and the ADP-ribosylating activity, cannot bind or be internalized, revealing the AB toxin-like property of MYPE9110. (See related article on p. 4362.)

Infect Immun. 2009 October; 77(10): Cover