The mucus components of the gut barrier are fortified by antimicrobial peptides and proteins including lysozyme.
Mucinous carcinomas are defined on the basis of the amount of the mucus component in the tumour mass.
The intestinal tissue specific knock out (ko) of this important cytoplasmatic TLR signalling compound leads for example to impaired antimicrobial activity and diminished levels of mucin-2 (the major mucus component), cumulating in differences in gut microbial composition, a greater number of mucus-associated bacteria, translocation events and increased colitis susceptibility (Frantz et al, 2012).
The reason for this effect on the main mucus component, the MUC2 mucin, is not understood.
The heterogeneity of mucus components offers a wide range of potential chemical interaction sites for macromolecules, while the mesh-like architecture given to mucus by the intermolecular cross-linking of mucin molecules results in a dense network that physically, and in a size-dependent manner, hinders the diffusion of nanoparticles through mucus.
Viscosity is the measure of the internal friction of a fluid caused by molecular attraction of major mucus components, especially mucins, non-mucin glycoprotein, and phospholipids.
Biochemical and genetic perturbations of HPV16 pseudovirions are therefore feasible; their interactions with defined mucus components and effects on virus motility can be studied directly.
Interactions with mucus components were determined within mucus diffusion studies and rheological investigations.
These genes included those categorized as mucus components, mucus-producing cell differentiation-related transcription factors, mucus-producing cell differentiation-related pathways or mediators, post-translational modification of mucin, vesicle transport, ER stress-associated, secretory granule-associated, mucus secretion-related regulators and mucus hypersecretory related ion channels.
Each protein has 5-11 cofies of a mucus-binding domain, as defined by Boekhorst et al [ 60], showing their particular role in binding to mucus components in the GI-tract [ 5, 70- 72].
