Structure of the nacreous organic matrix of a bivalve mollusk shell examined in the hydrated state using cryo-TEM.
During mollusk shell formation, the mineral phase forms within an organic matrix composed of beta-chitin, silk-like proteins, and acidic glycoproteins rich in aspartic acid. The matrix is widely assumed to play an important role in controlling mineralization. Thus, understanding its structure is of prime importance. Cryo-transmission electron microscopy (Cryo-TEM) studies of the matrix of the bivalve Atrina embedded in vitrified ice show that the interlamellar sheets are composed mainly of highly ordered and aligned beta-chitin fibrils. The silk, which is quantitatively an important component of the matrix, could not be imaged within the sheets. Organic material was, however, observed between sheets. We infer that this is the location of the silk. As this material reveals no regular structure, we suggest that at least prior to mineralization the silk is in the form of a hydrated gel. This is supported by cryo-TEM structural observations of an artificial assembly of beta-chitin with and without silk. This view of the nacreous organic matrix significantly changes previous models of the matrix structure and hence hypotheses pertaining to the mechanisms by which mineral formation occurs.
Levi-Kalisman
Y
Y
Department of Structural Biology, Weizmann Institute of Science, Rehovot, 76100, Israel.
Falini
G
G
Addadi
L
L
Weiner
S
S
D000818:Animals; D001224:Aspartic Acid; D002118:Calcium / Q000378:metabolism; D002686:Chitin / Q000032:analysis / Q000737:chemistry; D020285:Cryoelectron Microscopy / Q000379:methods; D005109:Extracellular Matrix / Q000648:ultrastructure; D005629:Frozen Sections; D006023:Glycoproteins / Q000737:chemistry*; D008974:Mollusca / Q000378:metabolism*; D011506:Proteins / Q000032:analysis / Q000378:metabolism*; D013194:Staining and Labeling; D014961:X-Ray Diffraction
D006023:Glycoproteins; D011506:Proteins; D002686:Chitin; D001224:Aspartic Acid; D002118:Calcium