scholarly journals The Structure and Function of Serum Opacity Factor: A Unique Streptococcal Virulence Determinant That Targets High-Density Lipoproteins

2010 ◽  
Vol 2010 ◽  
pp. 1-16 ◽  
Author(s):  
Harry S. Courtney ◽  
Henry J. Pownall
Keyword(s):  
Lipid Vesicles ◽  
Structure And Function ◽  
High Density ◽  
Host Cells ◽  
High Density Lipoproteins ◽  
Multifunctional Protein ◽  
Virulence Determinant ◽  
Serum Opacity Factor ◽  
Animal Pathogens ◽  
And Function

Serum opacity factor (SOF) is a virulence determinant expressed by a variety of streptococcal and staphylococcal species including both human and animal pathogens. SOF derives its name from its ability to opacify serum where it targets and disrupts the structure of high-density lipoproteins resulting in formation of large lipid vesicles that cause the serum to become cloudy. SOF is a multifunctional protein and in addition to its opacification activity, it binds to a number of host proteins that mediate adhesion of streptococci to host cells, and it plays a role in resistance to phagocytosis in human blood. This article will provide an overview of the structure and function of SOF, its role in the pathogenesis of streptococcal infections, its vaccine potential, its prevalence and distribution in bacteria, and the molecular mechanism whereby SOF opacifies serum and how an understanding of this mechanism may lead to therapies for reducing high-cholesterol concentrations in blood, a major risk factor for cardiovascular disease.

scholarly journals High-density lipoproteins for therapeutic delivery systems

2016 ◽  
Vol 4 (2) ◽  
pp. 188-197 ◽  
Author(s):  
R. Kannan Mutharasan ◽  
Linda Foit ◽  
C. Shad Thaxton
Keyword(s):  
Drug Delivery ◽  
Delivery Systems ◽  
Structure And Function ◽  
High Density ◽  
High Density Lipoproteins ◽  
Delivery Vehicle ◽  
Drug Delivery Vehicle ◽  
Therapeutic Delivery ◽  
And Function

High-density lipoproteins are a class of natural nanostructures with multiple desirable properties to model in a drug delivery vehicle. Here we review the structure and function of high-density lipoproteins, and their use as therapeutic delivery systems.

scholarly journals Effect of acylglyceride content on the structure and function of reconstituted high density lipoprotein particles

2001 ◽  
Vol 42 (1) ◽  
pp. 79-87 ◽  
Author(s):  
Sylvie Braschi ◽  
Cynthia R. Coffill ◽  
Tracey A-M. Neville ◽  
Darren M. Hutt ◽  
Daniel L. Sparks
Keyword(s):  
High Density Lipoprotein ◽  
Density Lipoprotein ◽  
Structure And Function ◽  
High Density ◽  
Lipoprotein Particles ◽  
And Function

Lipoprotein composition in NIDDM: effects of dietary oleic acid on the composition, oxidisability and function of low and high density lipoproteins

Diabetologia ◽  
1996 ◽  
Vol 39 (6) ◽  
pp. 667-676 ◽  
Author(s):  
E. Dimitriadis ◽  
M. Griffin ◽  
P. Collins ◽  
A. Johnson ◽  
D. Owens ◽  
...  
Keyword(s):  
Oleic Acid ◽  
High Density ◽  
High Density Lipoproteins ◽  
Lipoprotein Composition ◽  
And Function

scholarly journals Structure and function of accessory Sec proteins involved in the adhesin export pathway of Streptococcus gordonii

2017 ◽  
Author(s):  
Yu Chen ◽  
Barbara A. Bensing ◽  
Ravin Seepersaud ◽  
Wei Mi ◽  
Maofu Liao ◽  
...  
Keyword(s):  
Extracellular Matrix ◽  
Pathogenic Bacteria ◽  
Structure And Function ◽  
Host Cells ◽  
Carbohydrate Binding ◽  
Streptococcus Gordonii ◽  
Carbohydrate Binding Proteins ◽  
Sec Proteins ◽  
And Function ◽  
Complex Crystal

ABSTRACTMany pathogenic bacteria, including Streptococcus gordonii, possess a pathway for the export of a single serine-rich-repeat protein that mediates the adhesion of bacteria to host cells and the extracellular matrix. These adhesins are O-glycosylated by several cytosolic glycosyltransferases and require three accessory Sec proteins (Asp1-3) for export, but how the adhesins are processed for secretion is not well defined. Here, we show that O-glycosylation of S. gordonii adhesin GspB occurs in a sequential manner by three enzymes (GtfA/B, Nss, Gly) that attach N-acetylglucosamine and glucose to Ser/Thr residues. The modified substrate is subsequently transferred from the last glycosyltransferase to the Asp1/2/3 complex. Crystal structures show that both Asp1 and Asp3 are related to carbohydrate binding proteins. Asp1 also has an affinity for phospholipids, which is attenuated by Asp2. These results suggest a mechanism for the modification of adhesin in the cytosol and its subsequent targeting to the export machinery.

scholarly journals The Role of Meningococcal Porin B in Protein-Protein Interactions with Host Cells

2018 ◽  
Vol 62 (1) ◽  
pp. 52-58
Author(s):  
E. Káňová ◽  
I. Jiménez-Munguía ◽  
Ľ. Čomor ◽  
Z. Tkáčová ◽  
I. Širochmanová ◽  
...  
Keyword(s):  
Protein Interactions ◽  
Cell Signalling ◽  
Structure And Function ◽  
Host Cells ◽  
Protein Protein Interactions ◽  
Receptor Interactions ◽  
And Function ◽  
Fatal Sepsis ◽  
Porin B

Abstract Neisseria meningitidis is a Gram-negative diplococcus responsible for bacterial meningitis and fatal sepsis. Ligand-receptor interactions are one of the main steps in the development of neuroinvasion. Porin B (PorB), neisserial outer membrane protein (ligand), binds to host receptors and triggers many cell signalling cascades allowing the meningococcus to damage the host cells or induce immune cells responses via the TLR2-dependent mechanisms. In this paper, we present a brief review of the structure and function of PorB.

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