Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts:   Target Concepts:
Query: EC:3.2.1.17 (lysozyme)
 21,489 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The glycosyltransferase alpha-2,6-sialyltransferase (ST) is a Type II membrane protein localized to the Golgi apparatus. The first 44 amino acids of this protein were able to specify Golgi retention of a fused marker protein, lysozyme. This section of ST contains a transmembrane segment which serves as a non-cleaved signal anchor. When lysozyme was fused to an equivalent region of a cell surface protein it now appeared on the cell surface. Analysis of chimeras between the two proteins revealed that the transmembrane segment of ST specifies Golgi retention. Furthermore, altering this segment in full-length ST results in the protein accumulating on the cell surface. However, the retaining effect of the transmembrane domain of ST is augmented by the presence of adjacent lumenal and cytoplasmic sequences from ST. If these sequences are spaced apart by a transmembrane domain of the same length as that of ST they too can specify Golgi retention. Thus retention in the Golgi of ST appears to involve recognition of an extended region of the protein within and on both sides of the bilayer.
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PMID:Sequences within and adjacent to the transmembrane segment of alpha-2,6-sialyltransferase specify Golgi retention. 193 90

Interaction between CD4 cell surface protein and HIV-bearing gp120 has been described as the initial step for HIV entry into host cells. Some anti-CD4 antibodies were shown to inhibit this interaction. Biosensor studies using the BIAcore were performed to determine kinetic and thermodynamic parameters of the interaction of one of these antibodies (i.e. IOT4a, clone 13B8-2) with immobilized recombinant soluble CD4 (rsCD4). A non-linear regression method was used to analyze the sensorgrams, showing the existence of a double exponential time curve. A KA of 5.2 x 10(7) M-1 was calculated at 25 degrees C. The complex formation was exothermic (-4.5 kcal.mol-1( and entropically positive (+20 cal.mol-1.K-1). The reaction rate (0.234 x 10(5) M-1.s-1 at 25 degrees C) as well as the enthalpy change of the activated complex (+9.7 kcal.mol-1) are not compatible with a diffusion controlled reaction. The thermodynamic values calculated from equilibrium data corresponded to those calculated from kinetic data confirming the validity of the theoretical approach. As for most antigen-antibody interactions, complex formation was enthalpy driven. The overall positive entropy contribution to the stabilization of the complex is in contrast to that observed for the lysozyme-anti-lysozyme model and is probably due to electrostatic interaction between the epitope and the antibody combining site.
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PMID:Analysis of human CD4-antibody interaction using the BIAcore system. 760 32

Dental biofilm formation is critical for maintaining the healthy microbial ecology of the oral cavity. Streptococci are predominant bacterial species in the oral cavity and play important roles in the initiation of plaque formation. In this study, we identified a new cell surface protein, BapA1, from Streptococcus parasanguinis FW213 and determined that BapA1 is critical for biofilm formation. Sequence analysis revealed that BapA1 possesses a typical cell wall-sorting signal for cell surface-anchored proteins from Gram-positive bacteria. No functional orthologue was reported in other streptococci. BapA1 possesses nine putative pilin isopeptide linker domains which are crucial for pilus assembly in a number of Gram-positive bacteria. Deletion of the 3' portion of bapA1 generated a mutant that lacks surface-anchored BapA1 and abolishes formation of short fibrils on the cell surface. The mutant failed to form biofilms and exhibited reduced adherence to an in vitro tooth model. The BapA1 deficiency also inhibited bacterial autoaggregation. The N-terminal muramidase-released-protein-like domain mediated BapA1-BapA1 interactions, suggesting that BapA1-mediated cell-cell interactions are important for bacterial autoaggregation and biofilm formation. Furthermore, the BapA1-mediated bacterial adhesion and biofilm formation are independent of a fimbria-associated serine-rich repeat adhesin, Fap1, demonstrating that BapA1 is a new streptococcal adhesin.
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PMID:New cell surface protein involved in biofilm formation by Streptococcus parasanguinis. 2157 36