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An helicoidal structure surrounding the cilium axoneme: Visualization by the monoclonal antibody CC‐248
Author(s) -
BautistaHarris Guillermina,
Klotz Catherine,
Bordes Nicole,
Sandoz Daniel
Publication year - 1991
Publication title -
biology of the cell
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.543
H-Index - 85
eISSN - 1768-322X
pISSN - 0248-4900
DOI - 10.1016/0248-4900(91)90065-u
Subject(s) - axoneme , biology , cilium , cytoskeleton , intermediate filament , monoclonal antibody , microbiology and biotechnology , anatomy , protein filament , negative stain , biophysics , electron microscope , antibody , flagellum , cell , biochemistry , immunology , optics , gene , physics
Summary— Monoclonal antibody CC‐248 labels cilia differentially on Triton X‐100 permeabilized ciliated epithelium of quail oviduct by indirect immunofluorescence. On isolated ciliated cells, a punctuated staining is seen at the distal region over the bend of cilia. Electron micrographs of immunoperoxidase and immunogold techniques showed that the punctuated fluorescence corresponds to a helical disposition of CC‐248 antigenic sites. This labeling was arranged on the axonemal distal region either as a simple or a double helix externally disposed around the nine microtubular doublets. These results suggest the existence of a detergent insoluble structure in the ciliary matrix that might concern the ciliary skeleton, probably acting as an elastic recoil that keeps the structural integrity of the axoneme during bending. The cross‐reactivity of CC‐248 MAb with the intermediate filament cytoskeleton of ciliated and smooth muscle cells indicates that this structure might be related to the intermediate filament family.