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For hours, walk-ins and appointments.5 - 7 days
Turnaround time is defined as the usual number of days from the date of pickup of a specimen for testing to when the result is released to the ordering provider. In some cases, additional time should be allowed for additional confirmatory or additional reflex tests. Testing schedules may vary.
Gel-barrier tube or red-top tube
0.5 mL
0.1 mL (Note: This volume does not allow for repeat testing.)
If a red-top tube is used, transfer separated serum to a plastic transport tube.
Maintain specimen at room temperature. Stable 14 days. Stable refrigerated or frozen for 14 days. Freeze/thaw cycles: stable x3.
No special patient preparations are necessary.
Nonserum sample; hemolyzed or hyperlipemic sample received
The determination of MBL concentrations in serum may be useful for the elucidation of suspected immune defects and as a prognostic indicator alerting to the need for heightened therapeutic or prophylactic measures in immunosuppressed patients, including patients receiving cancer chemotherapy and patients with cystic fibrosis, SLE, or rheumatoid arthritis.
This test was developed and its performance characteristics determined by Labcorp. It has not been cleared or approved by the Food and Drug Administration.
Enzyme-linked immunosorbent assay (ELISA) using microwells coated with the unique monoclonal antibody to capture MBL via an epitope near its carbohydrate-binding site. Bound MBL is detected with the same antibody that has been labeled with biotin.
Mannose-binding lectin (MBL) is a multimeric, carbohydrate-binding protein produced in the liver and secreted into the blood that plays an important role in the innate immune response against invading microörganisms.1-6 MBL is a member of a family of the "collections" proteins, so named because they have a collagen-like region and a lectin region. Functional MBL is an oligomer complex of three identical monomer chains connected together through a triple helix of the collagen-like regions. The three C-terminal lectin carbohydrate recognition domains of the individual component proteins stick out from the triple helix in a manner that, by electron microscopy, resembles three flowers protruding from a single stalk. Many pathogens, including viruses, bacteria, fungi, protozoa, have surface sugars that are absent from mammalian cell surfaces. The lectin domains of the MBL complex recognize the spatial arrangement of carbohydrate sugar residues on pathogen surfaces and bind to them. Specific enzymes (MBL-associated serine proteases or MASPs) are activated when MBL binds to microbial carbohydrate surfaces and in turn activate complement via the MBL or lectin pathway. MBL binding to pathogens surfaces activates the complement system, causing inflammation, increased vascular permeability, and the recruitment and activation of phagocytes. MBL binding also facilities recognition and ingestion of the foreign entity by phagocytes in a process referred to as opsonization.
Only the normally oligomerized forms of MBL are capable of binding efficiently to the microbial carbohydrates and associating with the MASPs, thus activating complement via the lectin pathway. Diminished MBL levels can occur due to allelic variants in the promoter and/or structural regions of the MBL gene. Certain promoter alleles are associated with lower serum concentrations of MBL, while the structural variants impair both normal oligomerization of MBL and total chain synthesis.7 Subjects who are homozygous for a structural defect show very low levels of oligomerized MBL (<50 ng/mL), while heterozygotes show low-intermediate levels (50−500 ng/mL). In 100 healthy Danish blood donors, serum MBL concentrations determined by an oligomer-selective immunoassay showed low values (<50 ng/mL) in 12 individuals.8 Sallenbach and coworkers measured the MBL serum concentration in 631 apparently healthy subjects.9 The median MBL serum concentration was 1340 ng/mL (range, <5-12,200). Results were below the detection limit in 40 (11.4%) of 350 adults, in 1 of 141 preterm, and in 1 of 20 term neonates.9 Eisen and coworkers suggested that a cutoff of 500 ng/mL would be an appropriate threshold for identifying patients with MBL-deficient genotypes.10
Most individuals with diminished levels of normally oligomerized MBL are healthy with no clinical evidence of immune deficiency.11 While the consequences of MBL deficiency can be quite subtle, several studies have shown that MBL deficiency increases the overall susceptibility of an individual to infectious disease and predisposes to greater severity when infections occur. Decreased MBL levels may be associated with increased susceptibility to infections when the adaptive immune system is immature (in early childhood)12 or has been suppressed after organ transplantation13-15 or during cancer chemotherapy.16,17 In adults, MBL may play a role in determining host susceptibility to infection, pathogenesis, and progression of disease, and may contribute to the variability of host response to infection.10,18-20
Studies also suggest that individuals with relatively low MBL may suffer from more severe courses of autoimmune diseases such as systemic lupus erythematosus21,22 or rheumatoid arthritis,23 and from poorer prognoses in cystic fibrosis.24 Recurrent spontaneous abortions are reported to be correlated with low serum MBL levels.25,26 It has also been shown that low serum MBL levels have a negative impact on pregnancy outcome in women with a history of unexplained recurrent spontaneous abortion.27
Order Code | Order Code Name | Order Loinc | Result Code | Result Code Name | UofM | Result LOINC |
---|---|---|---|---|---|---|
004900 | Mannose Binding Lectin (MBL) | 000000 | ||||
004900 | Mannose Binding Lectin (MBL) | 004901 | Mannose Binding Lectin (MBL) | ng/mL | 30152-3 |
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