Antibodies to Native Type I and II Collagens Detected by an Enzyme linked Immunosorbent Assay (ELISA) in Rheumatoid Arthritis and Systemic Lupus Erythematosus

Gioud, M; Meghlaoui, A; Costa, Oscar Tadeu Ferreira da; Monier, J. C.

doi:10.1016/s0174-173x(82)80009-5

Cited by 25 publications

(16 citation statements)

References 18 publications

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“…This finding of an association between antibodies to NCII and expression of QRRAA may explain why some studies have found anti-CII antibodies to be associated with severe, active disease (31)(32)(33) and why an association was found between anti-NCII antibodies in synovial fluid and DR4 (3), since such patients would have had active disease at the time the sample was collected.…”

Section: Discussionmentioning

confidence: 97%

Antibodies to type II collagen and HLA disease susceptibility markers in rheumatoid arthritis

Cook

Stockman

Brand

et al. 1999

Arthritis & Rheumatism

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Objective. To seek associations between antibod-ies to native and denatured type II collagen (NCII and DCII) and HLA in rheumatoid arthritis (RA). Methods. One hundred fourteen patients with clinically well-defined RA were HLA-DR and DQ typed. Those who were DR4 positive were subtyped for DRB1*0401-*0408 alleles by polymerase chain reaction using allele-specific oligonucleotide probes. Antibodies to human NCII and DCII (heat-denatured) were measured by enzyme-linked immunosorbent assay. The frequency of HLA alleles was compared in patients grouped according to the presence and absence of antibodies to NCII and DCII. Results. Twenty-seven patients (24%) were positive for antibodies to NCII. There was a significant increase in the frequency of HLA-DR7 in anti-NCII-positive patients compared with anti-NCII-negative patients (30% versus 9%; P 0.019) and a significant decrease in HLA-DR3 (7% versus 28%; P 0.044). Repeating the analyses after excluding the 16 patients who were DR7 positive revealed a significant increase in the frequency of HLA-DR1 in anti-NCII-positive patients compared with anti-NCII-negative patients (63% versus 27%; P 0.045). Moreover, antibodies to NCII were associated with the third hypervariability region susceptibility sequence QRRAA that is present in DRB1*0101, *0404, *0405, and *0408 (84% versus 47%; P 0.0085); 24 of 27 anti-NCII-positive patients were positive for either DR7, DR1, or DRB1*0404 or *0408. Thirty patients (26%) were positive for antibodies to DCII. There was a significant increase in the frequency of HLA-DR3 in anti-DCII-positive patients compared with anti-DCII-negative patients (40% versus 18%; P 0.028). Conclusion. The genetic associations between HLA-DR alleles and antibodies to CII in RA patients is in keeping with the collagen-induced arthritis model and implicates autoimmunity to CII as a major component in the multifactorial pathogenesis of RA.

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Section: Discussionmentioning

confidence: 97%

Antibodies to type II collagen and HLA disease susceptibility markers in rheumatoid arthritis

Cook

Stockman

Brand

et al. 1999

Arthritis & Rheumatism

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“…For several autoimmune diseases, and specifically rheumatoid arthritis and systemic lupus erythematosus, common themes are the abnormal appearance of collagen within diseased sites and the presence of anticollagen antibodies in the patient's serum (13). Moreover, autoimmune diseases can be induced in experimental animals after exposure to collagen (7).…”

Section: Discussionmentioning

confidence: 99%

Recombinant Exosporium Protein BclA of Bacillus anthracis Is Effective as a Booster for Mice Primed with Suboptimal Amounts of Protective Antigen

et al. 2007

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Bacillus collagen-like protein of anthracis (BclA) is an immunodominant glycoprotein located on the exosporium of Bacillus anthracis. We hypothesized that antibodies to this spore surface antigen are largely responsible for the augmented immunity to anthrax that has been reported for animals vaccinated with inactivated spores and protective antigen (PA) compared to vaccination with PA alone. To test this theory, we first evaluated the capacity of recombinant, histidine-tagged, nonglycosylated BclA (rBclA) given with adjuvant to protect A/J mice against 10 times the 50% lethal dose of Sterne strain spores introduced subcutaneously. Although the animals elicited anti-rBclA antibodies and showed a slight but statistically significant prolongation in the mean time to death (MTD), none of the mice survived. Similarly, rabbit anti-rBclA immunoglobulin G (IgG) administered intraperitoneally to mice before spore inoculation increased the MTD statistically significantly but afforded protection to only 1 of 10 animals. However, all mice that received suboptimal amounts of recombinant PA and that then received rBclA 2 weeks later survived spore challenge. Additionally, anti-rBclA IgG, compared to anti-PA IgG, promoted a sevenfold-greater uptake of opsonized spores by mouse macrophages and markedly decreased intramacrophage spore germination. Since BclA has some sequence similarity to human collagen, we also tested the extent of binding of anti-rBclA antibodies to human collagen types I, III, and V and found no discernible cross-reactivity. Taken together, these results support the concept of rBclA as being a safe and effective boost for a PA-primed individual against anthrax and further suggest that such rBclA-enhanced protection occurs by the induction of spore-opsonizing and germination-inhibiting antibodies.Spores of Bacillus anthracis, the causative agent of anthrax, are the infectious form of the organism and can persist in soil in a dormant stage for decades (25). Although herbivores are the primary reservoir of anthrax, humans can contract anthrax, albeit rarely, if inoculated with spores cutaneously, orally, or inhalationally (8). Although anthrax is typically seen only in individuals involved in certain occupations, the potential for infection of larger numbers of people by the aerosol route is of public health concern because of the misuse of B. anthracis spores that occurred in the United States in 2001 (9).One way to protect vulnerable individuals and populations against anthrax is through a strategy of prophylactic immunization. Currently, the anthrax vaccine adsorbed (AVA) preparation is the only licensed anthrax vaccine for use in the United States. AVA is comprised of a formalin-treated, aluminum salt-adsorbed, cell-free culture filtrate from an attenuated strain of B. anthracis (3). Although AVA is considered to be safe and effective, the utility of the vaccine is limited by its availability, reactogenicity, requirement for the administration of multiple doses (3), and the generally adverse publicity that ...

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“…In addition, microbial infections are presumed to play a triggering role in several other autoimmune diseases (51). Interestingly, autoimmune diseases are often associated with elevated levels of anti-collagen antibodies present in patients' sera (52). Furthermore, autoimmune diseases can be induced in experimental animals treated with collagen (53).…”

Section: Discussionmentioning

confidence: 99%

Streptococcal Scl1 and Scl2 Proteins Form Collagen-like Triple Helices

Xu¹,

Keene²,

Bujnicki³

et al. 2002

Journal of Biological Chemistry

174

278

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The collagens are a family of animal proteins containing segments of repeated Gly-Xaa-Yaa (GXY) motifs that form a characteristic triple-helical structure. Genes encoding proteins with repeated GXY motifs have also been reported in bacteria and phages; however, it is unclear whether these prokaryotic proteins can form a collagen-like triple-helical structure. Here we used two recently identified streptococcal proteins, Scl1 and Scl2, containing extended GXY sequence repeats as model proteins. First we observed that prior to heat denaturation recombinant Scl proteins migrated as homotrimers in gel electrophoresis with and without SDS. We next showed that the collagen-like domain of Scl is resistant to proteolysis by trypsin. We further showed that circular dichroism spectra of the Scl proteins contained features characteristic of collagen triple helices, including a positive maximum of ellipticity at 220 nm. FurthermorethetriplehelicesofScl1andScl2showedatemperature-dependent unfolding with melting temperatures of 36.4 and 37.6°C, respectively, which resembles those seen for collagens. We finally demonstrated by electron microscopy that the Scl proteins are organized into "lollipoplike" structures, similar to those seen in human proteins with collagenous domains. This implies that the repeated GXY tripeptide motif is a structural indicator of collagenlike triple helices in proteins from such phylogenetically distant sources as bacteria and humans.The collagens comprise a large family of structurally related proteins that are essential building elements of connective tissues in animals (1). In addition to contributing to the structural integrity of the tissue, collagens may also affect cell behavior, e.g. by interacting with specific cellular receptors. All collagens contain a triple-helical domain composed of three left-handed polyproline II-type chains wound around the central axis to form a right-handed superhelix (2). The segments of the collagen polypeptide forming a triple helix contain the repeating amino acid sequence Gly-Xaa-Yaa (GXY) in which a glycine residue occupies every third position, since only glycine is small enough to be accommodated at the center of the triple helix. The three chains are linked by hydrogen bonds between the backbone group, -NH (Gly) and the backbone carbonyl group (X position) of another chain, and by water-mediated interactions. The X and Y positions are frequently occupied by the imino acids proline and hydroxyproline, respectively. Hydroxyprolines are formed by post-translational hydroxylation of proline residues and are important in stabilizing the collagen triple helix. In humans, mutations that affect collagen triple helix formation and fiber assembly have serious pathological consequences often leading to death (3).The vertebrate collagens are classified into 19 types that are grouped in two major categories known as fibrillar (types I-III, V, and XI) and nonfibrillar (IV, VI-X, and XII-XIX) collagens. In addition, a variety of other mammalian proteins have been identif...

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Antibodies to Native Type I and II Collagens Detected by an Enzyme linked Immunosorbent Assay (ELISA) in Rheumatoid Arthritis and Systemic Lupus Erythematosus

Cited by 25 publications

References 18 publications

Antibodies to type II collagen and HLA disease susceptibility markers in rheumatoid arthritis

Antibodies to type II collagen and HLA disease susceptibility markers in rheumatoid arthritis

Recombinant Exosporium Protein BclA of Bacillus anthracis Is Effective as a Booster for Mice Primed with Suboptimal Amounts of Protective Antigen

Streptococcal Scl1 and Scl2 Proteins Form Collagen-like Triple Helices

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