Glycosylation is a common modulation of protein function in eukaryotes and is biologically important. However, in bacteria protein glycosylation is rare, and relatively few bacterial glycoproteins are known. In Escherichia coli only two glycoproteins have been described to date. Here we introduce a novel member to this exclusive group, namely, antigen 43 (Ag43), a self-recognizing autotransport...

Little is known about the mechanisms that determine localization of proteins to the plasma membrane in Saccharomyces cerevisiae. The length of the transmembrane domains and association of proteins with lipid rafts have been proposed to play a role in sorting to the cell surface. Here, we report that Fus1p, an O-glycosylated integral membrane protein involved in cell fusion during yeast mating, ...

The nucleotide and amino acid sequences of the mRNA and predicted polypeptide of the integral membrane small hydrophobic (SH) protein of human respiratory syncytial virus strain 18537 (a prototype strain of antigenic subgroup B) were determined from cloned cDNA. At the nucleotide and amino acid levels there was 78% and 76% identity, respectively, with the previously described SH mRNA and protei...

objective(s):alzheimer's disease (ad) is the most common age-related neurodegenerative disorder. one of the hallmarks of ad is an abnormal accumulation of fibril forms of tau protein which is known as a microtubule associated protein. in this regard, inhibition of tau aggregation has been documented to be a potent therapeutic approach in ad and tauopathies. unfortunately, the available syn...

background: targeting of cd20 antigen with monoclonal antibodies has become the mainstay in the treatment of non-hodgkin's lymphomas and immunotherapeutic depletion of malignant b cells. accessibility of antigen is one of the crucial factors in development of monoclonal antibodies against this antigen. one major problem in expression of full length cd20 is aggregation and misfolding. there...

Conclusions Use of the drug tunicamycin has greatly facilitated study of many different aspects of immunoglobulin biosynthesis. The most striking conclusion is that blocking glycosylation does not prevent synthesis of immunoglobulin heavy chains either directly or by feedback; non-glycosylated heavy chains are able to assemble into immunoglobulin molecules capable of being secreted. Since glyco...

Soybean agglutinin (gSBA) is a tetrameric legume lectin, each of whose subunits are glycosylated. Earlier studies have shown that this protein shows exceptionally high stability in terms of free energy of unfolding when compared to other proteins from the same family. This article deals with the unfolding reactions of the nonglycosylated recombinant form of the protein rSBA and its comparison w...