Evolution of the mannose-binding lectin gene in primates

Falzacappa, Maria Vittoria Verga; Segat, Ludovica; Puppini, B; Amoroso, Antonio; Crovella, Sérgio

doi:10.1038/sj.gene.6364140

Cited by 16 publications

(13 citation statements)

References 31 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…The exon structure of the MBL2 gene is extremely well preserved between humans and other higher primates [49]. In particular, the homology in the collagen-like domain among primates is very high, and the MBL2 gene from primates seems not to carry analogue variants similar to those that are so prevalent in humans.…”

Section: Mbl2 Polymorphismsmentioning

confidence: 97%

Mannose-binding lectin genetics: from A to Z

Garred

2008

Biochemical Society Transactions

100

View full text Add to dashboard Cite

MBL (mannose-binding lectin) is primarily a liver-derived collagen-like serum protein. It binds sugar structures on micro-organisms and on dying host cells and is one of the four known mediators that initiate activation of the complement system via the lectin pathway. Common variant alleles situated both in promoter and structural regions of the human MBL gene (MBL2) influence the stability and the serum concentration of the protein. Epidemiological studies have suggested that genetically determined variations in MBL serum concentrations influence the susceptibility to and the course of different types of infectious, autoimmune, neoplastic, metabolic and cardiovascular diseases, but this is still a subject under discussion. The fact that these genetic variations are very frequent, indicates a dual role of MBL. This overview summarizes the current molecular understanding of human MBL2 genetics.

show abstract

Section: Mbl2 Polymorphismsmentioning

confidence: 97%

Mannose-binding lectin genetics: from A to Z

Garred

2008

Biochemical Society Transactions

100

View full text Add to dashboard Cite

show abstract

“…It has been shown that the exon structure in the MBL2 gene is extremely well preserved between human and higher primates. 49 In particular, the collagen-like domain is identical in humans, chimpanzees and gorillas at the amino-acid level and the difference in the whole protein is less than 1%. These few amino-acid differences do not result in changes of the structure or function of MBL.…”

Section: Historical Backgroundmentioning

confidence: 98%

Mannose-binding lectin and its genetic variants

et al. 2006

View full text Add to dashboard Cite

Mannose-binding lectin (MBL) is a collagen-like serum protein that mediates activation of the complement system and is of importance for host defence. Common variant alleles situated both in the promoter and structural region of the human MBL gene (MBL2) influence the stability and the serum concentration of the protein. Epidemiological studies have suggested that genetically determined variation in MBL serum concentration influences the susceptibility to and the course of different types of infections, autoimmune, metabolic and cardiovascular diseases, but this is still a subject of debate. The fact that these genetic variations are very frequent indicates a dual role for MBL in host defence. In this survey, we summarize the current molecular understanding of human MBL genetics.

show abstract

“…These results showed that intermediate forms were found in higher primates suggesting that the ancestral human MBL2 haplotype may have arisen in the evolutionary gap between LYQA and LYPA haplotypes. The exon structure of MBL2 is extremely well preserved between humans and higher primates . In particular the collagen‐like domain is almost identical, while some differences are observed in the CRD region.…”

Section: Mblmentioning

confidence: 99%

A journey through the lectin pathway of complement—MBL and beyond

Garred

Genster

Pilely

et al. 2016

Immunological Reviews

335

302

View full text Add to dashboard Cite

Mannose-binding lectin (MBL), collectin-10, collectin-11, and the ficolins (ficolin-1, ficolin-2, and ficolin-3) are soluble pattern recognition molecules in the lectin complement pathway. These proteins act as mediators of host defense and participate in maintenance of tissue homeostasis. They bind to conserved pathogen-specific structures and altered self-antigens and form complexes with the pentraxins to modulate innate immune functions. All molecules exhibit distinct expression in different tissue compartments, but all are found to a varying degree in the circulation. A common feature of these molecules is their ability to interact with a set of serine proteases named MASPs (MASP-1, MASP-2, and MASP-3). MASP-1 and -2 trigger the activation of the lectin pathway and MASP-3 may be involved in the activation of the alternative pathway of complement. Furthermore, MASPs mediate processes related to coagulation, bradykinin release, and endothelial and platelet activation. Variant alleles affecting expression and structure of the proteins have been associated with a variety of infectious and non-infectious diseases, most commonly as disease modifiers. Notably, the severe 3MC (Malpuech, Michels, Mingarelli, and Carnevale) embryonic development syndrome originates from rare mutations affecting either collectin-11 or MASP-3, indicating a broader functionality of the complement system than previously anticipated. This review summarizes the characteristics of the molecules in the lectin pathway.

show abstract

Evolution of the mannose-binding lectin gene in primates

Cited by 16 publications

References 31 publications

Mannose-binding lectin genetics: from A to Z

Mannose-binding lectin genetics: from A to Z

Mannose-binding lectin and its genetic variants

A journey through the lectin pathway of complement—MBL and beyond

Contact Info

Product

Resources

About