Changes in the pattern of cell surface proteins during transformation of bloodstream forms of Trypanosoma brucei in vitro

1990 ◽  
Vol 18 (5) ◽  
pp. 1032-1033 ◽  
Author(s):  
DAVID G. JACKSON ◽  
H. PAUL VOORHEIS
Keyword(s):  
Cell Surface ◽  
Trypanosoma Brucei ◽  
Surface Proteins ◽  
Cell Surface Proteins

scholarly journals Cell Surface Expression of Nrg1 Protein in Candida auris

2021 ◽  
Vol 7 (4) ◽  
pp. 262
Author(s):  
Anuja Paudyal ◽  
Govindsamy Vediyappan
Keyword(s):  
Cell Surface ◽  
Growth Conditions ◽  
Zinc Ion ◽  
Surface Proteins ◽  
Cell Surface Expression ◽  
Unexpected Finding ◽  
Candida Auris ◽  
Cell Surface Proteins ◽  
Biofilm Growth

Candida auris is an emerging antifungal resistant human fungal pathogen increasingly reported in healthcare facilities. It persists in hospital environments, and on skin surfaces, and can form biofilms readily. Here, we investigated the cell surface proteins from C. auris biofilms grown in a synthetic sweat medium mimicking human skin conditions. Cell surface proteins from both biofilm and planktonic control cells were extracted with a buffer containing β-mercaptoethanol and resolved by 2-D gel electrophoresis. Some of the differentially expressed proteins were excised and identified by mass spectrometry. C. albicans orthologs Spe3p, Tdh3p, Sod2p, Ywp1p, and Mdh1p were overexpressed in biofilm cells when compared to the planktonic cells of C. auris. Interestingly, several proteins with zinc ion binding activity were detected. Nrg1p is a zinc-binding transcription factor that negatively regulates hyphal growth in C. albicans. C. auris does not produce true hypha under standard in vitro growth conditions, and the role of Nrg1p in C. auris is currently unknown. Western blot analyses of cell surface and cytosolic proteins of C. auris against anti-CalNrg1 antibody revealed the Nrg1p in both locations. Cell surface localization of Nrg1p in C. auris, an unexpected finding, was further confirmed by immunofluorescence microscopy. Nrg1p expression is uniform across all four clades of C. auris and is dependent on growth conditions. Taken together, the data indicate that C. auris produces several unique proteins during its biofilm growth, which may assist in the skin-colonizing lifestyle of the fungus during its pathogenesis.

Laminin E8 alveolarization site: heparin sensitivity, cell surface receptors, and role in cell spreading

1997 ◽  
Vol 272 (3) ◽  
pp. L494-L503
Author(s):  
L. Chen ◽  
V. Shick ◽  
M. L. Matter ◽  
S. M. Laurie ◽  
R. C. Ogle ◽  
...  
Keyword(s):  
Cell Adhesion ◽  
Cell Surface ◽  
Surface Proteins ◽  
Cell Surface Proteins ◽  
Surface Receptors ◽  
Beta1 Integrin ◽  
Alpha Dystroglycan ◽  
Alveolar Formation ◽  
Laminin 1

Cell adhesion to amino acids 2179-2198 (SN-peptide) of the laminin-1 alpha1-chain is required for lung alveolar formation in vitro (M. L. Matter and G. W. Laurie. J. Cell Biol. 124: 1083-1090, 1994). The nature of the SN-peptide receptor(s) was probed with neutralizing anti-integrin monoclonal antibodies (MAb), cells lacking integrin subunits, soluble heparin, and SN-peptide columns. Cell adhesion and spreading studies confirmed the specificity of SN-peptide and revealed adhesion to be unaffected by inclusion of anti-beta1-, anti-alpha(2-6)- or anti-alpha(V)beta5-integrin MAb. Cells lacking beta1- or alpha6-integrin subunits were fully adherent. Adhesion was heparin, but not chondroitin sulfate or heparinase, sensitive, much as is alpha-dystroglycan-laminin-1 binding. Heparin eluted approximately 155- and 180-kDa cell-surface proteins from SN-peptide columns. An additional approximately 91-kDa protein was eluted by EDTA. All were unrecognized by anti-beta1-integrin MAb. SN-peptide therefore interacts with three cell-surface proteins for which the identity remains to be determined.

scholarly journals LYMPHOCYTE MEMBRANE DYNAMICS

1971 ◽  
Vol 134 (6) ◽  
pp. 1373-1384 ◽  
Author(s):  
Robert E. Cone ◽  
John J. Marchalonis ◽  
Ronald T. Rolley
Keyword(s):  
Cell Surface ◽  
Disc Electrophoresis ◽  
Membrane Dynamics ◽  
Surface Proteins ◽  
Dynamic State ◽  
Cellular Respiration ◽  
Spleen Cells ◽  
Cell Surface Proteins ◽  
Before And After

Cell surface proteins of normal and neoplastic lymphocytes were labeled with iodide-125I by lactoperoxidase-catalyzed iodination. Incubation of 125I-labeled iodide cells in vitro resulted in the release of iodinated surface proteins at a rapid rate which was dependent on cellular respiration and protein synthesis. Comparisons by disc electrophoresis showed a marked similarity between urea-soluble surface proteins extracted from iodinated cells and iodinated material released by the cells during in vitro incubation. The rate of release of cell surface proteins from thymus cells was three times faster than that of spleen cells or bone marrow-derived thoracic duct lymphocytes. In addition, different proteins were released at different rates as evidenced by the rate of release of 125I of rabbit anti-mouse immunoglobulin specifically bound to mouse spleen cells and comparisons by disc electrophoresis of urea-soluble iodinated surface proteins extracted from cells before and after incubation. The results suggest that a dynamic state exists at the cell surface. The possible role of the release of cell surface proteins in cell regulation and communication is discussed.

CHANGES IN CELL SURFACE PROTEINS DURING NORMAL AND VITAMIN A-INHIBITED CHONDROGENESIS IN VITRO

1978 ◽  
Vol 312 (1 Fibroblast Su) ◽  
pp. 406-409 ◽  
Author(s):  
J. R. Hassell ◽  
J. P. Pennypacker ◽  
K. M. Yamada ◽  
R. M. Pratt
Keyword(s):  
Vitamin A ◽  
Cell Surface ◽  
Surface Proteins ◽  
Cell Surface Proteins

Proteolytic release of cell surface proteins during differentiation of Trypanosoma brucei

Biochemistry ◽  
1993 ◽  
Vol 32 (14) ◽  
pp. 3737-3742 ◽  
Author(s):  
Karl Ziegelbauer ◽  
Bernd Stahl ◽  
Michael Karas ◽  
York Dieter Stierhof ◽  
Peter Overath
Keyword(s):  
Cell Surface ◽  
Trypanosoma Brucei ◽  
Surface Proteins ◽  
Cell Surface Proteins

scholarly journals Group II truncated haemoglobin YjbI prevents reactive oxygen species-induced protein aggregation in Bacillus subtilis

2021 ◽  
Author(s):  
Takeshi Imai ◽  
Ryuta Tobe ◽  
Koji Honda ◽  
Mai Tanaka ◽  
Jun Kawamoto ◽  
...  
Keyword(s):  
Reactive Oxygen Species ◽  
Bacillus Subtilis ◽  
Cell Surface ◽  
Matrix Protein ◽  
Reactive Oxygen ◽  
Surface Proteins ◽  
Oxygen Species ◽  
Cell Surface Proteins ◽  
Group Ii

Oxidative stress–mediated formation of protein hydroperoxides can induce irreversible fragmentation of the peptide backbone and accumulation of cross-linked protein aggregates, leading to cellular toxicity, dysfunction, and death. However, how bacteria protect themselves from damages caused by protein hydroperoxidisation is unknown. Here we show that YjbI, a group II truncated haemoglobin from Bacillus subtilis, prevents oxidative aggregation of cell-surface proteins by its biologically unprecedented protein hydroperoxide peroxidase-like activity, which removes hydroperoxide groups from oxidised proteins. Disruption of the yjbI gene in B. subtilis lowered biofilm water repellence and the mechanical stiffness of the cell surface, which associated with the cross-linked aggregation of the biofilm matrix protein TasA. YjbI was localised to the cell surface, and the sensitivity of planktonically grown cells to generators of reactive oxygen species was significantly increased upon yjbI disruption, suggesting that YjbI pleiotropically protects labile cell-surface proteins from oxidative damage. YjbI removed hydroperoxide residues from a model oxidised protein substrate, bovine serum albumin, and prevented its oxidative aggregation in vitro. These findings provide new insights into the role of truncated haemoglobin and the importance of hydroperoxide removal from proteins in the survival of aerobic bacteria.

scholarly journals Transmission of pseudorabies virus from immune-masked blood monocytes to endothelial cells

2003 ◽  
Vol 84 (3) ◽  
pp. 629-637 ◽  
Author(s):  
Gerlinde R. Van de Walle ◽  
Herman W. Favoreel ◽  
Hans J. Nauwynck ◽  
Thomas C. Mettenleiter ◽  
Maurice B. Pensaert
Keyword(s):  
Endothelial Cells ◽  
Cell Surface ◽  
Neutralizing Antibodies ◽  
Pseudorabies Virus ◽  
Surface Proteins ◽  
Blood Monocytes ◽  
Cell Surface Proteins ◽  
Pregnant Uterus ◽  
Specific Antibodies

Pseudorabies virus (PRV) may cause abortion, even in the presence of vaccination-induced immunity. Blood monocytes are essential to transport the virus in these immune animals, including transport to the pregnant uterus. Infected monocytes express viral proteins on their cell surface. Specific antibodies recognize these proteins and should activate antibody-dependent cell lysis. Previous work showed that addition of PRV-specific polyclonal antibodies to PRV-infected monocytes induced internalization of viral cell surface proteins, protecting the cells from efficient antibody-dependent lysis in vitro (immune-masked monocytes). As a first step to reach the pregnant uterus, PRV has to cross the endothelial cell barrier of the maternal blood vessels. The current aim was to investigate in vitro whether immune-masked PRV-infected monocytes can transmit PRV in the presence of virus-neutralizing antibodies via adhesion and fusion of these monocytes with endothelial cells. Porcine blood monocytes, infected with a lacZ-carrying PRV strain, were incubated with PRV-specific antibodies to induce internalization. Then, cells were co-cultivated with endothelial cells for different periods of time. Only PRV-infected monocytes with internalized viral cell surface proteins adhered efficiently to endothelial cells. LacZ transmission to endothelial cells, as a measure for monocyte–endothelial cell fusion, could be detected after co-cultivation from 30 min onwards. Virus transmission was confirmed by the appearance of plaques. Adhesion of immune-masked PRV-infected monocytes to endothelial cells was mediated by cellular adhesion complex CD11b–CD18 and subsequent fusion was mediated by the virus. In conclusion, immune-masked PRV-infected monocytes can adhere and subsequently transmit virus to endothelial cells in the presence of PRV-neutralizing antibodies.

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