Krzysztof P. Bzymek

Bio: Krzysztof P. Bzymek is an academic researcher from Beckman Research Institute. The author has contributed to research in topics: Binding site & Peptide. The author has an hindex of 12, co-authored 25 publications receiving 491 citations. Previous affiliations of Krzysztof P. Bzymek include University of California, San Diego & City of Hope National Medical Center.

Two translation products of Yersinia yscQ assemble to form a complex essential to type III secretion

Abstract: The bacterial flagellar C-ring is composed of two essential proteins, FliM and FliN The smaller protein, FliN, is similar to the C-terminus of the larger protein, FliM, both being composed of SpoA domains While bacterial type III secretion (T3S) systems encode many proteins in common with the flagellum, they mostly have a single protein in place of FliM and FliN This protein resembles FliM at its N-terminus and is as large as FliM but is more like FliN at its C-terminal SpoA domain We have discovered that a FliN-sized cognate indeed exists in the Yersinia T3S system to accompany the FliM-sized cognate The FliN-sized cognate, YscQ-C, is the product of an internal translation initiation site within the locus encoding the FliM-sized cognate YscQ Both intact YscQ and YscQ-C were found to be required for T3S, indicating that the internal translation initiation site, which is conserved in some but not all YscQ orthologs, is crucial for function The crystal structure of YscQ-C revealed a SpoA domain that

Meditopes and meditope-binding antibodies and uses thereof

Abstract: Antibodies and meditopes that bind to the antibodies are provided, as well as complexes, compositions and combinations containing the meditopes and antibodies, and methods of producing, using, testing, and screening the same, including therapeutic and diagnostic methods and uses.

Antibody therapy in cancer

Abstract: Monoclonal antibody (MoAb) for cancer treatment has been greatly progressed during this decade. Six kinds of MoAbs are now in clinical use in Japan. Here we review on the development of MoAbs such as rituximab, bevacizumab and cetuximab. The characterization and the nomenclature of MoAb are also described. Panitumumab, a new MoAb targeting epithelial growth factor receptor(EGFR), and the resistance of colorectal cancer with KRAS mutation for anti-EGFR MoAbs are on recent topics. The concept of bevacizumab beyond progression (BBP) and the unfavorable results of bevacizumab in elder nonsmall cell lung carcinoma patients are so suggestive considering the strategy of the individualized cancer therapy. Finally, "drug lag" for the development of anti-cancer agents between Eastern and Western has to be discussed.

Protein Export According to Schedule: Architecture, Assembly, and Regulation of Type III Secretion Systems from Plant- and Animal-Pathogenic Bacteria

Abstract: Flagellar and translocation-associated type III secretion (T3S) systems are present in most gram-negative plant- and animal-pathogenic bacteria and are often essential for bacterial motility or pathogenicity. The architectures of the complex membrane-spanning secretion apparatuses of both systems are similar, but they are associated with different extracellular appendages, including the flagellar hook and filament or the needle/pilus structures of translocation-associated T3S systems. The needle/pilus is connected to a bacterial translocon that is inserted into the host plasma membrane and mediates the transkingdom transport of bacterial effector proteins into eukaryotic cells. During the last 3 to 5 years, significant progress has been made in the characterization of membrane-associated core components and extracellular structures of T3S systems. Furthermore, transcriptional and posttranscriptional regulators that control T3S gene expression and substrate specificity have been described. Given the architecture of the T3S system, it is assumed that extracellular components of the secretion apparatus are secreted prior to effector proteins, suggesting that there is a hierarchy in T3S. The aim of this review is to summarize our current knowledge of T3S system components and associated control proteins from both plant- and animal-pathogenic bacteria.