CN110045126B - Biomarker for diagnosing autoimmune pancreatitis and application thereof - Google Patents
Biomarker for diagnosing autoimmune pancreatitis and application thereof Download PDFInfo
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- CN110045126B CN110045126B CN201910264499.XA CN201910264499A CN110045126B CN 110045126 B CN110045126 B CN 110045126B CN 201910264499 A CN201910264499 A CN 201910264499A CN 110045126 B CN110045126 B CN 110045126B
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- G01N33/00—Investigating or analysing materials by specific methods not covered by groups G01N1/00 - G01N31/00
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- G01N33/50—Chemical analysis of biological material, e.g. blood, urine; Testing involving biospecific ligand binding methods; Immunological testing
- G01N33/53—Immunoassay; Biospecific binding assay; Materials therefor
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- G01N33/00—Investigating or analysing materials by specific methods not covered by groups G01N1/00 - G01N31/00
- G01N33/48—Biological material, e.g. blood, urine; Haemocytometers
- G01N33/50—Chemical analysis of biological material, e.g. blood, urine; Testing involving biospecific ligand binding methods; Immunological testing
- G01N33/68—Chemical analysis of biological material, e.g. blood, urine; Testing involving biospecific ligand binding methods; Immunological testing involving proteins, peptides or amino acids
- G01N33/6854—Immunoglobulins
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- G—PHYSICS
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- G01N—INVESTIGATING OR ANALYSING MATERIALS BY DETERMINING THEIR CHEMICAL OR PHYSICAL PROPERTIES
- G01N33/00—Investigating or analysing materials by specific methods not covered by groups G01N1/00 - G01N31/00
- G01N33/48—Biological material, e.g. blood, urine; Haemocytometers
- G01N33/50—Chemical analysis of biological material, e.g. blood, urine; Testing involving biospecific ligand binding methods; Immunological testing
- G01N33/68—Chemical analysis of biological material, e.g. blood, urine; Testing involving biospecific ligand binding methods; Immunological testing involving proteins, peptides or amino acids
- G01N33/6893—Chemical analysis of biological material, e.g. blood, urine; Testing involving biospecific ligand binding methods; Immunological testing involving proteins, peptides or amino acids related to diseases not provided for elsewhere
Abstract
The invention discloses application of podophyllum kaempferi lectin in preparation of a reagent for diagnosing autoimmune pancreatitis. This study examined the glycan profile of serum IgG4 molecular surface specific binding to lectin in IgG4-RD patients using lectin microarrays and showed that LTL lectin-bound glycan levels were reduced in IgG4-RD patients. Since LTL lectin is specifically binding fucose, this suggests that the expression of fucose glycosylation levels is reduced in IgG4-RD patients. Further study of IgG4-RD glycosylation expression in three subgroups showed that LTL lectin-binding glycan levels were the lowest expressed in patients with autoimmune pancreatitis, indicating that LTL lectin-binding glycan levels could be used as a biomarker for diagnosis of autoimmune pancreatitis diseases.
Description
Technical Field
The invention belongs to the field of biological detection, and particularly relates to a biomarker for diagnosing autoimmune pancreatitis and application thereof.
Background
Glycosylation is one of the most common forms of post-transcriptional modification of proteins. Glycosylation can affect protein-protein interactions, cell-cell recognition, adhesion, and chemotaxis. There is increasing evidence that changes in glycosylation in disease states are associated with the development of diseases, such as tumors, autoimmune diseases. Thus, analysis of the type of glycoprotein glycosylation can improve specificity in disease diagnosis
IgG 4-related diseases (IgG4 related diseases, IgG4RD) are a new immune-mediated autoinflammatory disease recognized in recent years. The disease is mainly characterized by hyperplasia and swelling of affected organs or tissues, obviously increased serum IgG4 level (>1350mg/L), and IgG4 positive lymphocyte infiltration in the affected tissues (IgG4 positive plasma cells account for more than 50% of total plasma cells). The disease can affect a plurality of organs or tissues such as lacrimal gland, salivary gland, pancreas, retroperitoneal tissue, bile duct, lung, kidney, prostate and the like, and is clinically manifested as miculitz disease, autoimmune pancreatitis, retroperitoneal fibrosis, autoimmune cholangitis, interstitial pneumonia, periorbital inflammatory pseudotumor and the like. The journal of the 2010 autoimmune disease review (Autoimmunity Reviews) is titled "birth of a new syndrome: the clinical spectrum of IgG 4-related diseases "announces this new disease species as recognized. The comprehensive diagnosis standard of the disease is published for the first time in the international year of 2012, so that the diagnosis of the disease is standardized. The pathology characterized by IgG4-RD is characterized by lymphocyte infiltration, basket fibrosis, and obliterative phlebitis. The IgG4-RD can be used for early diagnosis and early treatment, and can prevent serious organ damage, tissue fibrosis and even death.
The glycoprotein concentration in human serum is about 40g/L, which is an excellent source for finding biomarkers of human diseases. Unlike RNA and proteins, synthesis of glycans attached to glycoproteins does not require a template. Glycosylation is a process influenced by a variety of factors, including: cell type and its activation state; environmental factors, such as the presence of available metabolites; age of the cell, as part of the glycans may be lost over time; inflammatory mediators, such as cytokines and chemokines. All of these factors may be altered in the context of autoimmunity. For example, some autoimmune diseases have characteristic cytokines. These cytokines have an effect on the expression of glycosidases, sialidases and glycosyltransferases, which directly affect glycan synthesis. Theoretically, a characteristic immune state can be manifested in the glycosylation of serum glycoproteins.
In view of the important role of glycosylation in diseases, the expression of serum IgG4 glycosylation of IgG4-RD patients is screened by a high-throughput glycosylation analysis technology, namely a lectin microarray, so as to investigate the clinical application value of glycosylation in IgG 4-RD.
Disclosure of Invention
In order to solve the above problems, the present invention provides a biomarker for diagnosing autoimmune pancreatitis and uses thereof.
First, the present invention provides a biomarker for diagnosing autoimmune pancreatitis, which is a complex formed by binding of passion fruit agglutinin and IgG 4.
Wherein, the IgG4 contains fucoidan.
Secondly, the invention also provides application of the marker in preparing a reagent for diagnosing autoimmune pancreatitis.
Specifically, the diagnosis includes: determining the level of a complex formed by binding of crowtoe lectin to IgG4 in a biological sample obtained from a patient exhibiting an IgG 4-related disease; optionally, the step of (a) is carried out,
comparing the level of complex formed by binding of paullinia cupana with IgG4 in the biological sample to control data, wherein a detectably reduced level of complex formed by binding of paullinia cupana with IgG4 in the sample relative to the control data is indicative of a likelihood of developing autoimmune pancreatitis.
Wherein the biological sample is a serum sample.
Preferably, the level of complex formed by the binding of podophyllum kawachii lectin to IgG4 is measured by the steps comprising:
a. contacting a biological sample from a patient with Lotus wingpod agglutinin;
b. forming a lectin-glycan complex between IgG4 present in the biological sample and the paullinia cupana lectin;
c. washing to remove any unbound IgG 4;
d. adding a detection antibody that is labeled and reactive with an antibody from the biological sample;
e. washing to remove any unbound labeled detection antibody; and
f. converting the label of the detection antibody to a detectable signal. Secondly, the invention also provides application of the podophyllum kaempferi lectin in preparing a reagent for diagnosing autoimmune pancreatitis.
Wherein, the Leptospermum heterophyllum agglutinin is deposited or fixed on a solid phase surface carrier.
The solid phase surface carrier is preferably in any form of latex beads, porous plates or membrane strips, nano-tubes, flakes with two-dimensional codes and the like.
Wherein the detection antibody is labeled by covalent attachment to an enzyme, a label with a fluorescent compound or metal, or a label with a chemiluminescent compound.
In another aspect, the invention also provides the use of podagra lectin in the preparation of a reagent for diagnosing autoimmune pancreatitis.
Wherein the diagnosing comprises: contacting paullinia cupana with a biological sample determined from a patient exhibiting an IgG 4-related disease to determine the level of complexes formed by binding of paullinia cupana to IgG 4; optionally, the first and second coating layers are formed by coating,
comparing the level of complex formed by binding of paullinia cupana with IgG4 in the biological sample to control data, wherein a detectably reduced level of complex formed by binding of paullinia cupana with IgG4 in the sample relative to the control data indicates a likelihood of multi-organ involvement in the development of an IgG 4-related disease.
Wherein the biological sample is a serum sample.
Preferably, the level of complex formed by the binding of podophyllum kawachii lectin to IgG4 is measured by the steps comprising:
a. contacting a biological sample from a patient with Lotus wingpod agglutinin;
b. forming a lectin-glycan complex between IgG4 present in the biological sample and the paullinia cupana lectin;
c. washing to remove any unbound IgG 4;
d. adding a detection antibody that is labeled and reactive with an antibody from the biological sample;
e. washing to remove any unbound labeled detection antibody; and
f. converting the label of the detection antibody to a detectable signal. Secondly, the invention also provides application of the podophyllum kaempferi lectin in preparing a reagent for diagnosing autoimmune pancreatitis.
Wherein, the Leptospermum heterophyllum agglutinin is deposited or fixed on a solid phase surface carrier.
The solid phase surface carrier is preferably in any form of latex beads, porous plates or membrane strips, nano-tubes, flakes with two-dimensional codes and the like.
Wherein the detection antibody is labeled by covalent attachment to an enzyme, a label with a fluorescent compound or metal, or a label with a chemiluminescent compound.
In another aspect, the present invention also provides a kit for detecting and/or quantifying IgG4 capable of binding to crowtoe lectin in a biological sample, comprising: a solid phase surface carrier, wherein the passion fruit agglutinin is deposited or fixed on the solid phase surface carrier, and a complex formed by the bonding of the passion fruit agglutinin and IgG4 is used as a biomarker of autoimmune pancreatitis.
In a preferred embodiment of the invention, the kit further comprises a detection antibody that is labeled and reactive with an antibody from the biological sample.
Preferably, the solid phase surface carrier is any form of latex beads, porous plates or membrane strips, nano-tubes, flakes with two-dimensional codes and the like.
The results of this study, which determined the glycan profile of serum IgG4 molecules surface specific to lectin from IgG4-RD patients by using lectin microarrays, showed that LTL lectin-bound glycan levels were reduced in IgG4-RD patients. Since LTL lectin is specifically binding fucose, this suggests that the expression of fucose glycosylation levels is reduced in IgG4-RD patients. Three subgroups were further studied for IgG4-RD glycosylation expression, and the results showed that LTL lectin binding glycan levels were minimally expressed in patients with autoimmune pancreatitis.
The results of the study show that LTL lectin-binding glycan levels are reduced in IgG4-RD patients, particularly in autoimmune pancreatitis patients, and that LTL lectin-binding glycan levels can be used as a biological marker for diagnosis of autoimmune pancreatitis diseases.
Drawings
FIG. 1 shows the layout of a microarray of 56 lectins (triplicate wells) on an array slide.
FIG. 2 is a schematic drawing of IgG4-RD patient lectin microarray.
FIG. 3 comparison of LTL lectin signal values in IgG4-RD group, DC group and HC group (. times.. P < 0.01).
FIG. 4 shows a comparison of LTL lectin signal values and ROC plots for autoimmune pancreatitis and DC patients.
FIG. 5 shows a comparison of LTL lectin signal values and ROC plots for autoimmune pancreatitis and HC patients.
FIG. 6 shows the correlation of IgG4 concentration before and after purification.
FIG. 7 shows the correlation of LTL lectin signal values between serum IgG4 and purified IgG4 in a lectin microarray.
Detailed Description
The following examples are intended to illustrate the invention but are not intended to limit the scope of the invention.
Experimental specimen: three groups of people included in this study included: IgG4-RD group (167 patients IgG4-RD, 59 patients with melez disease in group a1, 50 patients with autoimmune pancreatitis in group a2, 58 patients with retroperitoneal fibrosis in group A3), DC group (130 AID disease controls), HC group (86 healthy subjects). Wherein the diagnosis of the IgG4-RD group and the DC group meets the diagnosis standard of the corresponding diseases. All the people who entered the group collected fresh blood, and immediately separated serum, and frozen at-80 ℃ for later use.
Example 1 lectin microarray analysis of serum IgG4 glycosylation
A lectin microarray consisting of 56 lectin microchips. 56 lectins were fixed in triplicate on a chip, and the total serum from each patient was diluted 1:1000, added to the array, and incubated overnight at 4 ℃. Then, anti-IgG 4-Cy3 conjugate was hybridized to the microchip in the dark for 45 minutes. The fluorescence intensity of all proteins and the fluorescence intensity of low signals were analyzed independently. The chip image is converted to a digital format for analysis.
The signal-to-noise ratio (S/N) of each lectin spot was calculated using its signal-to-noise ratio (moderate intensity of spot foreground versus background). To prevent bias of lectin microarrays between arrays, we normalized the S/N data using normalization between arrays. Significant differences in lectin binding activity were determined by the distribution of data within the groups according to the following rules (1) the mean S/N of the lectins in the IgG4-RD group should not be less than the maximum S/N in the control group (50% (IgG4-RD group) ≧ Max (control group)); (2) the lower quartile of S/N in the IgG4-RD group should not be less than the upper quartile of the control group (25% (IgG4-RD group) ≥ 75% (control group); 3) the minimum S/N in the IgG4-RD group should not be less than the median of the control group [ minimum (IgG4-RD group) ≥ 50% (control group) ].
A lectin microarray containing 56 lectins was used to detect the glycosylation state in the experimental samples (FIG. 1). The lectin can be specifically combined with glycan molecules at the tail end of the glycoprotein to form a complex, and the type and content of the glycan on the surface of the target protein can be researched through the specific combination of different lectins and the glycan. Lectin microarrays are now being widely used in glycosylation research due to their high efficiency. After the frozen samples are balanced at room temperature, the samples are added into a lectin microarray to react with the lectin microarray, and then the signal value of each lectin and the specific binding glycan thereof can be obtained through the steps of washing, sealing, fluorescent secondary antibody reaction, fluorescence detection and the like, wherein the signal value is related to the binding affinity and the binding strength (figure 2).
To ensure that the collected fluorescent signal was derived from a specific binding of IgG4, the IgG4 antibody was labeled with Cy 3. The lectin S/N data, which fit any of the three aforementioned rules, was identified as significantly different, for a total of 6 lectins (table 1).
TABLE 1 lectins with significant differences in lectin microarrays
The affinity signal values for the 6 lectins showed significant differences between the three groups of samples. By lectin-glycan binding signal analysis, we found that whereas the Lotus Tetragonolobus Lectin (LTL) signal values were overall reduced in the IgG4-RD group compared to the DC and HC groups (fig. 3), further analysis of the distribution of LTL lectin signal values in the IgG4-RD subgroup found that autoimmune pancreatitis in the a2 subgroup was the lowest in the three subgroups (data and ROC plots as in fig. 4-5). Given the specific binding of LTL to fucose (Fuc) glycans, we concluded that IgG4-RD patients, particularly autoimmune pancreatitis patients, exhibited a reduced tendency to have IgG4 fucosylation in their serum compared to other groups and could be used as a biological marker for diagnosis and differential diagnosis of autoimmune pancreatitis.
Example 2 serum IgG4 purification and characterization
To further determine whether changes in glycosylation in IgG-RD patients were due to increased serum IgG4 concentrations, or actual changes in glycosylation, a second lectin microarray and a lectin blot Dotblot were used for validation. The second lectin is composed of 6 lectins including HPA, DSL, LTL, VVA mannose, MNA-M and ConA. The operation is the same as before.
IgG4 was isolated from serum by immunoprecipitation. Samples included 12 IgG-RD patients, 3 DC patients and 1 HC patient. Mu.l of mouse anti-IgG 4 antibody (southern Biotech, Birmingham, USA) was coupled to 20. mu.l of beads (NHS-activated Sepharose) TM 4F ast Flow, GE healthcare Life Sciences, Pittsburgh, USA), howeverThen 0.1M Tris-HCl was added to seal the excess sites. The murine anti-IgG 4 antibody beads were washed 3 times with acidic and basic solutions. Mu.l serum was used per column. The column was incubated overnight. After 8 washes with PBST and 2 washes with water, IgG4 was eluted into the vacuum tube with 20. mu.l of 0.1M glycine. Protein purity was characterized by Dotblot, protein concentration was determined by protein silver staining kit (Beyotiome, shanghai, china), and all IgG4 samples were stored at-80 ℃ for subsequent processing.
By comparing the purified IgG4 concentration and the relative serum IgG4 content in 16 patients, it was found that the purified IgG4 concentration results in a better correlation with serum IgG4 levels (r ═ 0.593, P ═ 0.015) (fig. 6). The results show that for LTL lectin, signal values for serum IgG4 microarray were directly proportional to those of purified IgG4 microarray (fig. 7). This indicates that the level of fucose glycosylation, a LTL lectin-bound glycan, is abnormal in the serum of IgG4-RD patients.
Example 3167 correlation analysis of IgG4 glycosylation with laboratory characteristics in IgG-RD patients
Significant differences were observed between lectin signals in IgG-RD patients, and we further evaluated the relationship between lectin signals and clinical laboratory indices. The correlation analysis results show that: LTL lectin-bound glycan levels in IgG4-RD patients were positively correlated with serum IgA levels (Table 2).
TABLE 2167 correlation of lectin-bound glycan content of IgG4-RD patients with laboratory characterization
NS without significant difference
Example 4167 IgG-RD patients relationship of IgG4 glycosylation to organ involvement
Different levels of lectin-specific binding glycans were compared in patients presenting with various organ involvement. The results are shown in Table 3. This indicates that LTL lectin-binding glycan levels in IgG4-RD patients are associated with polycystic pancreas, bile duct involvement and retroperitoneal fibrosis (Table 3). The results show that LTL-bound glycan levels are statistically different in patients with and without involvement of pancreatic, biliary and retroperitoneal fibrosis in these organs, and that the clinical features of autoimmune pancreatitis are also manifested by involvement of these organs. Thereby providing evidence for the index to diagnose autoimmune pancreatitis.
TABLE 3 comparison of organ involvement with IgG4 glycosylation content in IgG4-RD patients
NS no significant difference.
Claims (9)
1. Use of a biomarker which is a complex formed by binding of Lotus japonicus lectin to IgG4 in the preparation of a reagent for diagnosing autoimmune pancreatitis.
2. The use of claim 1, wherein said diagnosing comprises: determining the level of a complex formed by binding of crowtoe lectin to IgG4 in a biological sample obtained from a patient exhibiting an IgG 4-related disease; comparing the level of complex formed by binding of paullinia cupana with IgG4 in the biological sample to control data, wherein a detectably reduced level of complex formed by binding of paullinia cupana with IgG4 in the sample relative to the control data is indicative of a likelihood of developing autoimmune pancreatitis.
3. Use of agglutinin of centella asiatica in the preparation of a reagent for diagnosing autoimmune pancreatitis.
4. The use of claim 3, wherein said diagnosing comprises: contacting paullinia cupana with a biological sample determined from a patient exhibiting an IgG 4-related disease to determine the level of complexes formed by binding of paullinia cupana to IgG 4; comparing the level of complex formed by binding of paullinia cupana with IgG4 in the biological sample to control data, wherein a detectably reduced level of complex formed by binding of paullinia cupana with IgG4 in the sample relative to the control data is indicative of a likelihood of developing autoimmune pancreatitis.
5. The use of claim 2 or 4, wherein the biological sample is a serum sample.
6. The use of claim 2 or 4, wherein the level of complex formed by binding of Potentilla wingpod lectin to IgG4 is measured by the steps comprising: a. contacting a biological sample from a patient with Lotus wingpod agglutinin; b. forming a lectin-glycan complex between IgG4 present in the biological sample and the paullinia cupana lectin; c. washing to remove any unbound IgG 4; d. adding a detection antibody that is labeled and reactive with an antibody from the biological sample; e. washing to remove any unbound labeled detection antibody; converting the label of the detection antibody to a detectable signal.
7. The use of claim 6, wherein the Potentilla wingaefolia lectin is deposited or immobilized on a solid surface support.
8. The use according to claim 7, wherein the solid surface support is in the form of latex beads, porous plates or membrane strips, nanotubes, flakes with two-dimensional codes.
9. The use of claim 6, wherein the detection antibody is covalently linked to an enzyme, a label with a fluorescent compound or metal, or a label with a chemiluminescent compound.
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