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Glycoprotein 340, Carbohydrate epitope, MUC7 (saliva), Clone 213_01, Mab anti_Human; ELISA_WB_IH

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[#HYB213-01] Glycoprotein 340, Carbohydrate epitope, MUC7 (saliva), Clone 213_01, Mab anti_Human; ELISA_WB_IH


HYB213-01 | Glycoprotein 340, Carbohydrate epitope, MUC7 (saliva), Clone 213_01, Mab anti_Human; ELISA_WB_IH, 200 µg.
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(1) Monoclonal antibody-assisted structure-function analysis of the carbohydrate recognition domain of surfactant protein D.[TOP]

Pubmed ID :20601494
Publication Date : //
Surfactant protein D (SP-D) plays important roles in host defense against a variety of pathogens including influenza A virus (IAV). Ligand binding by SP-D is mediated by the trimeric neck and carbohydrate recognition domain (NCRD). We used monoclonal antibodies (mAbs) against human SP-D and a panel of mutant collectin NCRD constructs to identify functionally and structurally important epitopes. The ability of SP-D to bind to IAV and mannan involved partially overlapping binding sites that are distinct from those involved in binding to the glycoprotein-340 (gp-340) scavenger receptor protein. A species-specific motif (D324,D325,R343), which has been implicated in the specific binding of several ligands, contributes to recognition by mAbs that block antiviral or mannan binding activity. D325, in particular, is involved in the epitopes of these blocking mAbs. Conversely, the interspecies substitution of arginine for Lys343 in the rat NCRD (rK343R) conferred binding to two of the mAbs. The single site substitution of alanine for R349 or E347 resulted in highly selective alterations in mAb binding and caused decreased antiviral activity. Mutations at Glu333 (E333A), Trp340 (W340F), and Phe335 (F335A), which abrogated antiviral activity, were associated with decreased binding to multiple blocking mAbs, consistent with critical structural roles. More conservative substitutions at 335, which showed a significant increase in neutralization activity, caused selective loss of binding to one mAb. The analysis reveals, for the first time, an extended binding site for IAV; calcium-dependent antiviral activity involves residues flanking the primary carbohydrate binding site as well as more remote residues displayed on the carbohydrate recognition domain surface.

Authors : Hartshorn Kevan L, White Mitchell R, Rynkiewicz Michael, Sorensen Grith, Holmskov Uffe, Head James, Crouch Erika C,

(2) Glycosylation as a target for recognition of influenza viruses by the innate immune system.[TOP]

Pubmed ID :17892219
Publication Date : //
Glycosylation clearly plays an important role in the life cycle of influenza viruses and certain glycosylation sites are required for the structural integrity and stability of the HA and NA glycoproteins during biosynthesis and formation of intact virions. Furthermore, glycosylation has been shown to modulate the functions of influenza glycoproteins, in particular the recognition of host cell receptors and in shielding antigenic epitopes on the viral HA. The addition of oligosaccharide moieties to the globular head of the HA does, however, correlate with an increased sensitivity to the antiviral activities of SP-D and to recognition and destruction of virus via the MMR on murine macrophages. Consequently, the degree of glycosylation appears to be an important factor in determining sensitivity to lectin-mediated defences, and therefore in determining the ability of a particular virus strain to replicate in the respiratory tract of mice following intranasal infection. The mouse-adapted PR8 strain which lacks mannose-containing glycans from the head of its HA molecule was largely resistant to the antiviral activities of SP-D and the MMR in vitro and induced severed clinical disease following intranasal infection of mice. The finding that mannan treatment of BJx109-infected mice facilitated an early and dramatic enhancement of disease severity is also consistent with a major role for mannose-specific lectins in limiting influenza virus growth and spread in the respiratory tract.

Authors : Reading Patrick C, Tate Michelle D, Pickett Danielle L, Brooks Andrew G,

(3) Immunohistochemical detection of salivary agglutinin/gp-340 in human parotid, submandibular, and labial salivary glands.[TOP]

Pubmed ID :11829014
Publication Date : //
Salivary agglutinin is a Streptococcus mutans binding protein and a member of the scavenger receptor cysteine-rich superfamily. It is identical to lung gp-340 and brain DMBT1, which possibly play a role in innate immunity and tumor suppression, respectively. The goal of this study was to localize salivary agglutinin in human salivary glands. Two monoclonal antibodies, directed against gp-340, were characterized. mAb 213-1 reacted with sialic acid epitopes and cross-reacted with MUC7. The reaction with mAb 213-6 disappeared after reduction, suggesting that a protein epitope was recognized. In the parotid gland, immunohistochemical labeling with mAb 213-6 was found in the duct cells. In the submandibular gland and labial gland, both serous acini and demilune cells were labeled. In the labial gland, labeling was found at the luminal side of the duct cells. Salivary agglutinin was distinctly localized in salivary glands, but in distinct glandular secretions, no differences in electrophoretic behavior were observed.

Authors : Bikker F J, Ligtenberg A J M, van der Wal J E, van den Keijbus P A M, Holmskov U, Veerman E C I, Nieuw Amerongen A V,

(4) Salivary agglutinin, which binds Streptococcus mutans and Helicobacter pylori, is the lung scavenger receptor cysteine-rich protein gp-340.[TOP]

Pubmed ID :11007786
Publication Date : //
Salivary agglutinin is a high molecular mass component of human saliva that binds Streptococcus mutans, an oral bacterium implicated in dental caries. To study its protein sequence, we isolated the agglutinin from human parotid saliva. After trypsin digestion, a portion was analyzed by matrix-assisted laser/desorption ionization time-of-flight mass spectrometry (MALDI-TOF MS), which gave the molecular mass of 14 unique peptides. The remainder of the digest was subjected to high performance liquid chromatography, and the separated peptides were analyzed by MALDI-TOF/post-source decay; the spectra gave the sequences of five peptides. The molecular mass and peptide sequence information showed that salivary agglutinin peptides were identical to sequences in lung (lavage) gp-340, a member of the scavenger receptor cysteine-rich protein family. Immunoblotting with antibodies that specifically recognized either lung gp-340 or the agglutinin confirmed that the salivary agglutinin was gp-340. Immunoblotting with an antibody specific to the sialyl Le(x) carbohydrate epitope detected expression on the salivary but not the lung glycoprotein, possible evidence of different glycoforms. The salivary agglutinin also interacted with Helicobacter pylori, implicated in gastritis and peptic ulcer disease, Streptococcus agalactiae, implicated in neonatal meningitis, and several oral commensal streptococci. These results identify the salivary agglutinin as gp-340 and suggest it binds bacteria that are important determinants of either the oral ecology or systemic diseases.

Authors : Prakobphol A, Xu F, Hoang V M, Larsson T, Bergstrom J, Johansson I, Frängsmyr L, Holmskov U, Leffler H, Nilsson C, Borén T, Wright J R, Strömberg N, Fisher S J,