Lubricin: A novel means to decrease bacterial adhesion and proliferation

Abstract

This study investigated the ability of lubricin (LUB) to prevent bacterial attachment and proliferation on model tissue culture polystyrene surfaces. The findings from this study indicated that LUB was able to reduce the attachment and growth of Staphylococcus aureus on tissue culture polystyrene over the course of 24 h by approximately 13.9% compared to a phosphate buffered saline (PBS)-soaked control. LUB also increased S. aureus lag time (the period of time between the introduction of bacteria to a new environment and their exponential growth) by approximately 27% compared to a PBS-soaked control. This study also indicated that vitronectin (VTN), a protein homologous to LUB, reduced bacterial S. aureus adhesion and growth on tissue culture polystyrene by approximately 11% compared to a PBS-soaked control. VTN also increased the lag time of S. aureus by approximately 43%, compared to a PBS-soaked control. Bovine submaxillary mucin was studied because there are similarities between it and the center mucin-like domain of LUB. Results showed that the reduction of S. aureus and Staphylococcus epidermidis proliferation on mucin coated surfaces was not as substantial as that seen with LUB. In summary, this study provided the first evidence that LUB reduced the initial adhesion and growth of both S. aureus and S. epidermidis on a model surface to suppress biofilm formation. These reductions in initial bacteria adhesion and proliferation can be beneficial for medical implants and, although requiring more study, can lead to drastically improved patient outcomes.

Lubricin on Platinum Electrodes: A Low‐Impedance Protein‐Resistant Surface Towards Biomedical Implantation

“…The LUB central fragment is a mucin domain with high glycosylation, in which short glycan oligomers terminated mostly by polar galactose and negatively charged sialic acid are O‐linked to serine and threonine residues. The central mucin domain imparts LUB's lubrication and anti‐adhesive properties . Both ends of the mucin domain are lightly glycosylated “end domains” of the protein which contain sub domains similar to two globular proteins, homeopexin and somatomedin‐B .…”

Proteoglycan 4 reduces friction more than other synovial fluid components for both cartilage-cartilage and cartilage-metal articulation

“…Finally, since this study confirms the presence of PRG4 in joint fluid of patients with artificial joints, prostheses and implants can benefit from a coating which allows the formation of boundary layers. A PRG4-covered surface imparts a negatively charged hydrophilic nature on the coated surface and can promote the formation of an aqueous fluid film [14], [45]. Therefore, experimental optimization of functionalized surfaces of cartilage resurfacing implants should be explored by making use of coatings.…”

Lubricin Antiadhesive Coatings Exhibit Size‐Selective Transport Properties that Inhibit Biofouling of Electrode Surfaces with Minimal Loss in Electrochemical Activity

“…The majority of the LUB molecule's length is derived from the heavy glycosylated central portion that is commonly referred to as the “mucin domain.” Within this mucin domain, short glycan oligomers terminated primarily by polar galactose (≈33% of total glycans) and negatively charged sialic acid (≈66% of total glycans) are O‐linked to threonine and serine residues . This central mucin domain is responsible for LUB's excellent lubrication and antiadhesive properties . Flanking either end of the central mucin domain are two globular and highly adhesive “end domains,” which contain subdomains similar to two proteins, somatomedin‐B and hemopexin, known also to be present in extracellular adhesion proteins such as vitronectin .…”