Salted fish products from the Coptic monastery at Bawit, Egypt: evidence from the bones and texts

Fish bone assemblages are described that were recently discovered in the storage area of two rooms, dated to the 7th century AD, from the monastery of Bawit, Egypt. The species composition, the reconstructed sizes of the fish and the find contexts show that this material represents pickled fish (salsamenta). This product was made in one case of medium-sized Clarias catfish, whereas another assemblage, found inside an amphora, consisted of small-sized fish, mainly cyprinids and alestiids. The latter product was stored in a Late Roman Amphora 5/6 of Palestinian origin, traditionally considered as a container for wine. The amphora was clearly re-used since the fish found in it are Nilotic species which excludes that the salsamenta came from outside Egypt. A few additional finds of fish inside amphorae were available, but due to the low number of bones it was unclear if salted fish products were stored in them. Textual information provided by ostraca and papyri from the same site shows that the monks exerted fishing activities themselves and also suggests that the production of pickled fish took place locally. One of the two Nilotic fish taxa (Labeo) that is specifically mentioned by written evidence is the most common ingredient found in the amphora with abundant fish remains. The paper ends with a brief summary of other faunal evidence for salted fish products from monastic and other historic sites in Egypt.

The F4 fimbrial chaperone FaeE is stable as a monomer that does not require self-capping of its pilin-interactive surfaces.

Many Gram-negative bacteria use the chaperone-usher pathway to express adhesive surface structures, such as fimbriae, in order to mediate attachment to host cells. Periplasmic chaperones are required to shuttle fimbrial subunits or pilins through the periplasmic space in an assembly-competent form. The chaperones cap the hydrophobic surface of the pilins through a donor-strand complementation mechanism. FaeE is the periplasmic chaperone required for the assembly of the F4 fimbriae of enterotoxigenic Escherichia coli. The FaeE crystal structure shows a dimer formed by interaction between the pilin-binding interfaces of the two monomers. Dimerization and tetramerization have been observed previously in crystal structures of fimbrial chaperones and have been suggested to serve as a self-capping mechanism that protects the pilin-interactive surfaces in solution in the absence of the pilins. However, thermodynamic and biochemical data show that FaeE occurs as a stable monomer in solution. Other lines of evidence indicate that self-capping of the pilin-interactive interfaces is not a mechanism that is conservedly applied by all periplasmic chaperones, but is rather a case-specific solution to cap aggregation-prone surfaces.