V

Vincent A. Fischetti

Rockefeller University

ORCID: 0000-0003-3743-2002

Publishes on Streptococcal Infections and Treatments, Bacteriophages and microbial interactions, Antimicrobial Resistance in Staphylococcus. 308 papers and 25.2k citations.

308Publications
25.2kTotal Citations

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Gram-Positive Pathogens
Cited by 1k

specimen handling is emphasised but exact descriptions of smear preparation are not provided.) The final three chapters deal with principles of safe practice, including the role of clinical cytology in patient management, medicolegal considerations, and the contentious issue of the relative merits of fine needle aspiration and core biopsy. The intervening chapters are about specific areas of concern in practice, such as cystic lesions, lymphoid infiltrates and small round cell tumors. It should be apparent that I like this book very much, and it does succeed in its purpose of restating the potential and problems of clinical cytopathology in a way that provides both orientation for the neophyte and advice for the practicing pathologist. Having said that, there are occasional jarring things about it. An inexplicable number of spelling errors are present, including one on the first page! A few sub-standard photomicrographs appear to have been gleaned from other sources, and other photomicrographs seem to be a ‘‘poor fit’’ with the findings described in the text. But these are minor considerations. I intend to have trainees in my institution read the first few chapters several times during their time with the cytology service, and would certainly highly recommend this book to all practicing pathologists having any involvement with cytopathology.

Streptococcal M protein: molecular design and biological behavior
Vincent A. Fischetti|Clinical Microbiology Reviews|1989
Cited by 812Open Access

M protein is a major virulence determinant for the group A streptococcus by virtue of its ability to allow the organism to resist phagocytosis. Common in eucaryotes, the fibrillar coiled-coil design for the M molecule may prove to be a common motif for surface proteins in gram-positive organisms. This type of structure offers the organism several distinct advantages, ranging from antigenic variation to multiple functional domains. The close resemblance of this molecular design to that of certain mammalian proteins could help explain on a molecular level the formation of epitopes responsible for serological cross-reactions between microbial and mammalian proteins. Many of the approaches described in the elucidation of the M-protein structure may be applied for characterizing similar molecules in other microbial systems.