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GAPDH, beta-galactosidase, enolase (COG0148; central carbohydrate metabolism), phosphoglycerate mutase (COG0588; central carbohydrate metabolism) and elongation factor Tu (COG 0050) have all been noted to mediate binding to host mucins, fibrinogen, and/or plasminogen [38] [43].
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F. tularensis employs bacterial surface proteins to colonize the host cells by binding to specific host-cell receptors.
The IL2 activity of the fusion protein to induce proliferation of activated T cells is still conserved after binding to MUC1 mucin (cf. Figure 8).
Early experiments suggested that S. aureus binding to mucin may be critical for colonization of the nasophyngeal mucosa [ 37].
In Lactobacillus johnsonii and Listeria monocytogenes, EF-Tu is also associated to the membrane; in these bacteria this protein mediates binding to mucin [ 44] and fibrinogen [ 37], respectively.
It specifically recognizes the constant fraction of IgG, and plays a relevant role in the structural maintenance of the mucosa through the binding to the MUC2 mucin [ 39].
When the dietary polysaccharides became less available, the bacterium turned to the utilization of the host mucins.
FimH mediates binding to mannose containing host receptors.
By binding to T cell immunoglobulin mucin-3 (TIM-3) on activated Th1 cells, galectin-9 (Gal-9) negatively regulates Th1-type alloimmunity.
As mucins are strategically positioned between the vulnerable mucosa and the bacterial contents of the intestinal lumen [46], the changes in mucin concentrations and the consequent changes in mucin binding to bacteria are likely to affect both host-commensal and host-pathogen interactions.
(E) PBZ treatment does not affect the binding of HCV to host cells.
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