MBL2 : mannose binding lectin 2
Description
The MBL2 (mannose binding lectin 2) is a protein-coding gene located on chromosome 10.
The MBL2 gene provides instructions for producing a protein that forms a complex called mannose-binding lectin. This complex consists of two to six trimers, each composed of three subunits derived from the MBL2 gene. Mannose-binding lectin plays a vital role in the immune response to foreign invaders (pathogens). It recognizes and binds to sugars like mannose, fucose, and glucose found on the surfaces of bacteria, viruses, and yeast. This binding activates the complement system, a group of immune proteins that destroy pathogens, trigger inflammation, and remove cell debris. Mannose-binding lectin also targets pathogens for engulfment and breakdown by specialized immune cells, providing a crucial first line of defense against infection.
MBL2 protein acts as a calcium-dependent lectin in the innate immune system. It recognizes and binds to sugars like mannose, fucose, and N-acetylglucosamine on the surfaces of various microorganisms, triggering the lectin complement pathway. This pathway helps eliminate pathogens and reduce inflammation. MBL2 also binds to late apoptotic cells and necrotic cells, facilitating their removal by macrophages. It may interact with DNA and has been shown to inhibit the catalytic activity of MEP1A and MEP1B. During SARS-CoV-2 infection, MBL2 activates the complement lectin pathway, inhibiting viral infection and reducing inflammatory responses.
MBL2 is also known as COLEC1, HSMBPC, MBL, MBL2D, MBP, MBP-C, MBP1, MBPD.