The PSII-S Protein of Higher Plants: A New Type of Pigment-Binding Protein

Biochemistry ◽  
1995 ◽  
Vol 34 (35) ◽  
pp. 11133-11141 ◽  
Author(s):  
Christiane Funk ◽  
Wolfgang P. Schroeder ◽  
Artur Napiwotzki ◽  
Staffan E. Tjus ◽  
Gernot Renger ◽  
...  
Keyword(s):  
Higher Plants ◽  
Binding Protein ◽  
S Protein ◽  
New Type

scholarly journals "Peptabody": A new type of high avidity binding protein

1997 ◽  
Vol 94 (5) ◽  
pp. 1663-1668 ◽  
Author(s):  
A. V. Terskikh ◽  
J.-M. Le Doussal ◽  
R. Crameri ◽  
I. Fisch ◽  
J.-P. Mach ◽  
...  
Keyword(s):  
Binding Protein ◽  
High Avidity ◽  
New Type

Nucleotide sequence ofCab-8, a new type I gene encoding a chlorophylla/b-binding protein of LHC II inPisum

1991 ◽  
Vol 17 (3) ◽  
pp. 523-526 ◽  
Author(s):  
Laura Alexander ◽  
Denis Falconet ◽  
Brian W. Fristensky ◽  
Michael J. White ◽  
John C. Watson ◽  
...  
Keyword(s):  
Nucleotide Sequence ◽  
Binding Protein ◽  
Type I ◽  
Gene Encoding ◽  
Lhc Ii ◽  
New Type ◽  
I Gene

scholarly journals Establishment of murine hybridoma cells producing antibodies against spike protein of SARS-CoV-2

2020 ◽  
Author(s):  
Nadezhda V. Antipova ◽  
Tatyana D. Larionova ◽  
Michail I. Shakhparonov ◽  
Marat S. Pavlyukov
Keyword(s):  
Genetically Engineered ◽  
Local Source ◽  
Hybridoma Cells ◽  
Enzyme Linked Immunosorbent Assay ◽  
Molecular Tools ◽  
S Protein ◽  
Heavy Chains ◽  
New Type ◽  
Binding Sequence

AbstractIn 2020 the world faced the pandemic of COVID-19 - severe acute respiratory syndrome caused by a new type of coronavirus named SARS-CoV-2. To stop the spread of the disease, it is crucial to create molecular tools allowing to investigate, diagnose and treat COVID-19. One of such tools are monoclonal antibodies (mAbs). In this study we describe the development of hybridoma cells that can produce mouse mAbs against receptor binding domain of SARS-CoV-2 spike (S) protein. These mAbs are able to specifically detect native and denaturized S protein in all tested applications including immunoblotting, immunofluorescence staining and enzyme-linked immunosorbent assay. In addition, we showed that the obtained mAbs decreased infection rate of human cells by SARS-CoV-2 pseudovirus particles in in vitro experiments. Finally, we determined the amino acid sequence of light and heavy chains of the mAbs. This information will allow to use the corresponding peptides to establish genetically engineered therapeutic antibodies. To date multiple mAbs against SARS-CoV-2 proteins have been established, however due to the restrictions caused by pandemic, it is imperative to have a local source of the antibodies suitable for researches and diagnostics of COVID-19. Moreover, as each mAb has a unique binding sequence, bigger sets of various antibodies will allow to detect SARS-CoV-2 proteins even if the virus acquires novel mutations.

scholarly journals Inhibition of ribulose bisphosphate carboxylase assembly by antibody to a binding protein.

1986 ◽  
Vol 103 (4) ◽  
pp. 1327-1335 ◽  
Author(s):  
S Cannon ◽  
P Wang ◽  
H Roy
Keyword(s):  
Higher Plants ◽  
Binding Protein ◽  
Large Subunit ◽  
Ribulose Bisphosphate Carboxylase ◽  
Ribulose Bisphosphate ◽  
Dual Effect ◽  
Bisphosphate Carboxylase ◽  
Low Concentrations ◽  
The One

We have developed an assay to monitor in vitro the posttranslational assembly of the chloroplast protein, ribulose-1,5-bisphosphate carboxylase/oxygenase (RuBisCO). Most of the newly synthesized 55-kD catalytic ("large") subunits of this enzyme occur in a 29S complex together with 60- and 61-kD "binding" proteins. When the 29S complex is incubated with ATP and MgCl2 it dissociates into subunits, and the formerly bound large subunits now sediment at 7S (still faster than expected for a monomer). Upon incubation at 24 degrees C, these large subunits assemble into RuBisCO. The minority of newly made large subunits which are not bound to the 29S complex also sediment at 7S. When endogenous ATP was removed by addition of hexokinase and glucose, the dissociation of the 29S complex was inhibited. Nevertheless, the 7S large subunits assembled into RuBisCO, and did so to a greater extent than in controls retaining endogenous ATP. Thus the 7S large subunits are also assembly competent, at least when ATP is removed. Apparently, in chloroplast extracts, ATP can have a dual effect on the assembly of RuBisCO: on the one hand, even at low concentrations it can inhibit incorporation of 7S large subunits RuBisCO; on the other hand, at higher concentrations it can lead to substantial buildup of the 7S large subunit pool by causing dissociation of the 29S complex, and stimulate overall assembly. At both high and zero concentrations of ATP, however, antibody to the binding protein inhibited the assembly of endogenous large subunits into RuBisCO. Thus it appears that all assembly-competent large subunits are associated with the binding protein, either in the 7S complex or in the 29S complex. The involvement of the binding protein in RuBisCO assembly may represent the first example of non-autonomous protein assembly in higher plants and may pose problems for the genetic engineering of RuBisCO from these organisms.

scholarly journals LPS-binding protein and CD14-dependent attachment of hepatitis B surface antigen to monocytes is determined by the phospholipid moiety of the particles

2002 ◽  
Vol 83 (9) ◽  
pp. 2279-2289 ◽  
Author(s):  
Peter Vanlandschoot ◽  
Freya Van Houtte ◽  
Annelies Roobrouck ◽  
Ali Farhoudi ◽  
Felix Stelter ◽  
...  
Keyword(s):  
Hepatitis B ◽  
Surface Antigen ◽  
Binding Protein ◽  
Hepatitis B Surface Antigen ◽  
Binding Pocket ◽  
Receptor Interaction ◽  
S Protein ◽  
Hbv Vaccine ◽  
B Virus ◽  
Lps Binding

It was observed recently that recombinant yeast-derived hepatitis B surface antigen (rHBsAg) particles, which contain the S protein only, bind almost exclusively to monocytes. It is shown here that binding requires the presence of the LPS receptor CD14. Furthermore, evidence is presented that a domain on CD14 that is identical to or largely overlaps with the LPS-binding pocket is instrumental for the attachment of rHBsAg. Additionally, it is shown that the heat-labile LPS-binding protein (LBP) catalyses the binding of rHBsAg to the cells. Remarkably, natural plasma-derived HBsAg (pHBsAg) does not have this property. pHBsAg devoid of its lipids and reconstituted with phosphatidylserine or phosphatidylglycerol acquires the characteristic of yeast-derived HBsAg. Clearly, the interaction of rHBsAg with the cell membrane is determined by the presence of charged phospholipids that are absent in pHBsAg. Although a lipid–receptor interaction is suggested, antibody-inhibition experiments suggest a possible involvement of the C-terminal region of the S protein in the interaction with monocytes. The possible implications of these observations for hepatitis B virus (HBV) infection and HBV vaccine efficiency are discussed.

scholarly journals A non-canonical mechanism for Crm1-export cargo complex assembly

eLife ◽  
2015 ◽  
Vol 4 ◽  
Author(s):  
Ute Fischer ◽  
Nico Schäuble ◽  
Sabina Schütz ◽  
Martin Altvater ◽  
Yiming Chang ◽  
...  
Keyword(s):  
Complex Formation ◽  
Nuclear Export ◽  
Binding Protein ◽  
Complex Assembly ◽  
Stepwise Mechanism ◽  
Weak Binding ◽  
New Type ◽  
Ribosome Export ◽  
Transport Receptor

The transport receptor Crm1 mediates the export of diverse cargos containing leucine-rich nuclear export signals (NESs) through complex formation with RanGTP. To ensure efficient cargo release in the cytoplasm, NESs have evolved to display low affinity for Crm1. However, mechanisms that overcome low affinity to assemble Crm1-export complexes in the nucleus remain poorly understood. In this study, we reveal a new type of RanGTP-binding protein, Slx9, which facilitates Crm1 recruitment to the 40S pre-ribosome-associated NES-containing adaptor Rio2. In vitro, Slx9 binds Rio2 and RanGTP, forming a complex. This complex directly loads Crm1, unveiling a non-canonical stepwise mechanism to assemble a Crm1-export complex. A mutation in Slx9 that impairs Crm1-export complex assembly inhibits 40S pre-ribosome export. Thus, Slx9 functions as a scaffold to optimally present RanGTP and the NES to Crm1, therefore, triggering 40S pre-ribosome export. This mechanism could represent one solution to the paradox of weak binding events underlying rapid Crm1-mediated export.

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