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. 2017 Feb 21;8:114. doi: 10.3389/fimmu.2017.00114

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Copyright © 2017 Hyde.

This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution or reproduction in other forums is permitted, provided the original author(s) or licensor are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms.

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Proteolytic activity may promote Borrelia burgdorferi invasion of the extracellular matrix. B. burgdorferi (Bb) protease BbHtrA cleaves the family of hyalectin proteoglycans that includes hyalectin family of chondroitin sulfate proteoglycans, including aggrecan, brevican, neurocan, and versican. Specifically, BbHtrA protease activity degrades aggrecan (green lines) as indicated by dotted green line. This activity may contribute to ECM degradation and allow invasion of the pathogen. The presence of B. burgdorferi induces host matrix metalloproteases (MMP) from endothelial cells, chondrocytes, neutrophils, lymphoblast, and keratinocytes. Collagen (red lines) is degraded (dotted red line) by MMP-1 that is transcriptionally regulated along with MMP-3 through the JNK, mitogen-activated protein kinase, and JAK/STAT pathways.