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Wyszukujesz frazę "Domain" wg kryterium: Temat


Tytuł:
Human plasma and cerebrospinal fibronectins differ in the accessibility of the epitopes on the N-terminal domains
Autorzy:
Pupek, Małgorzata
Lemańska-Perek, Anna
Jasonek, Jolanta
Kątnik-Prastowska, Iwona
Powiązania:
https://bibliotekanauki.pl/articles/1040377.pdf
Data publikacji:
2010
Wydawca:
Polskie Towarzystwo Biochemiczne
Tematy:
cerebrospinal fluid
cell-binding fibronectin domain
N-terminal fibronectin domain
C-terminal fibronectin domain
fibronectin
Opis:
Three monoclonal antibodies specific to the central cell-binding and the C- and N-terminal domains of fibronectin (FN) were used to test antigenic epitope accessibility on human plasma and cerebrospinal fibronectins. In the plasma group, the mean N-terminal FN domain immunoreactivity was about one fourth that of the cell-binding and C-terminal domains, whereas in cerebrospinal fluid they were nearly equal. In the presence of 0.5-6 M urea N-terminal domain immunoreactivity in the plasma increased 3-6-fold, but it decreased 0.7-3-fold in the cerebrospinal fluid. Analysis of fibronectin domain immunoreactivities of the cell-binding and N-terminal domains by a panel of specific monoclonal antibodies may reveal N-terminal fibronectin domain accessibility for reaction with biological partner ligand(s) and/or processes in which FN could be implicated. Such determinations may have important clinical implications.
Źródło:
Acta Biochimica Polonica; 2010, 57, 3; 333-337
0001-527X
Pojawia się w:
Acta Biochimica Polonica
Dostawca treści:
Biblioteka Nauki
Artykuł
Tytuł:
Structural basis of the interspecies interaction between the chaperone DnaK(Hsp70) and the co-chaperone GrpE of archaea and bacteria
Autorzy:
Żmijewski, Michał
Skórko-Glonek, Joanna
Tanfani, Fabio
Banecki, Bogdan
Kotlarz, Agnieszka
Macario, Alberto
Lipińska, Barbara
Powiązania:
https://bibliotekanauki.pl/articles/1041069.pdf
Data publikacji:
2007
Wydawca:
Polskie Towarzystwo Biochemiczne
Tematy:
substrate-binding domain
DnaK-GrpE complex
archaeal Hsp70(DnaK)
archaeal DnaK structure
molecular chaperones
ATPase domain
Opis:
Hsp70s are chaperone proteins that are conserved in evolution and present in all prokaryotic and eukaryotic organisms. In the archaea, which form a distinct kingdom, the Hsp70 chaperones have been found in some species only, including Methanosarcina mazei. Both the bacterial and archaeal Hsp70(DnaK) chaperones cooperate with a GrpE co-chaperone which stimulates the ATPase activity of the DnaK protein. It is currently believed that the archaeal Hsp70 system was obtained by the lateral transfer of chaperone genes from bacteria. Our previous finding that the DnaK and GrpE proteins of M. mazei can functionally cooperate with the Escherichia coli GrpE and DnaK supported this hypothesis. However, the cooperation was surprising, considering the very low identity of the GrpE proteins (26%) and the relatively low identity of the DnaK proteins (56%). The aim of this work was to investigate the molecular basis of the observed interspecies chaperone interaction. Infrared resolution-enhanced spectra of the M. mazei and E. coli DnaK proteins were almost identical, indicating high similarity of their secondary structures, however, some small differences in band position and in the intensity of amide I' band components were observed and discussed. Profiles of thermal denaturation of both proteins were similar, although they indicated a higher thermostability of the M. mazei DnaK compared to the E. coli DnaK. Electrophoresis under non-denaturing conditions demonstrated that purified DnaK and GrpE of E. coli and M. mazei formed mixed complexes. Protein modeling revealed high similarity of the 3-dimensional structures of the archaeal and bacterial DnaK and GrpE proteins.
Źródło:
Acta Biochimica Polonica; 2007, 54, 2; 245-252
0001-527X
Pojawia się w:
Acta Biochimica Polonica
Dostawca treści:
Biblioteka Nauki
Artykuł
Tytuł:
Structure, function, and regulation of myosin 1C.
Autorzy:
Barylko, Barbara
Jung, Gwanghyun
Albanesi, Joseph
Powiązania:
https://bibliotekanauki.pl/articles/1041416.pdf
Data publikacji:
2005
Wydawca:
Polskie Towarzystwo Biochemiczne
Tematy:
myosin 1
membrane protein translocation
domain structure
Opis:
Myosin 1C, the first mammalian single-headed myosin to be purified, cloned, and sequenced, has been implicated in the translocation of plasma membrane channels and transporters. Like other forms of myosin I (of which eight exist in humans) myosin 1C consists of motor, neck, and tail domains. The neck domain binds calmodulins more tightly in the absence than in the presence of Ca^(2+). Release of calmodulins exposes binding sites for anionic lipids, particularly phosphoinositides. The tail domain, which has an isoelectic point of 10.5, interacts with anionic lipid headgroups. When both neck and tail lipid binding sites are engaged, the myosin associates essentially irreversibly with membranes. Despite this tight membrane binding, it is widely believed that myosin 1C docking proteins are necessary for targeting the enzyme to specific subcellular location. The search for these putative myosin 1C receptors is an active area of research.
Źródło:
Acta Biochimica Polonica; 2005, 52, 2; 373-380
0001-527X
Pojawia się w:
Acta Biochimica Polonica
Dostawca treści:
Biblioteka Nauki
Artykuł
Tytuł:
PDZ domains - common players in the cell signaling.
Autorzy:
Jeleń, Filip
Oleksy, Arkadiusz
Śmietana, Katarzyna
Otlewski, Jacek
Powiązania:
https://bibliotekanauki.pl/articles/1043370.pdf
Data publikacji:
2003
Wydawca:
Polskie Towarzystwo Biochemiczne
Tematy:
PDZ domain
module
protein-protein interaction
signaling
Opis:
PDZ domains are ubiquitous protein interaction modules that play a key role in cellular signaling. Their binding specificity involves recognition of the carboxyl-terminus of various proteins, often belonging to receptor and ion channel families. PDZ domains also mediate more complicated molecular networks through PDZ-PDZ interactions, recognition of internal protein sequences or phosphatidylinositol moieties. The domains often form a tandem of multiple copies, but equally often such tandems or single PDZ domain occur in combination with other signaling domains (for example SH3, DH/PH, GUK, LIM, CaMK). Common occurrence of PDZ domains in Metazoans strongly suggests that their evolutionary appearance results from the complication of signaling mechanisms in multicellular organisms. Here, we focus on their structure, specificity and role in signaling pathways.
Źródło:
Acta Biochimica Polonica; 2003, 50, 4; 985-1017
0001-527X
Pojawia się w:
Acta Biochimica Polonica
Dostawca treści:
Biblioteka Nauki
Artykuł
Tytuł:
Antitumor effect of RGD-4C-GG-D(KLAKLAK)2 peptide in mouse B16(F10) melanoma model
Autorzy:
Smolarczyk, Ryszard
Cichoń, Tomasz
Graja, Klaudyna
Hucz, Joanna
Sochanik, Aleksander
Szala, Stanisław
Powiązania:
https://bibliotekanauki.pl/articles/1041177.pdf
Data publikacji:
2006
Wydawca:
Polskie Towarzystwo Biochemiczne
Tematy:
antivascular therapy
two-domain peptides
anticancer therapy
Opis:
Vasculature targeting agents have been tested as cancer therapeutics for the past few years. Such therapy could be accomplished using, for example, bifunctional (two-domain) peptides. RGD-4C-GG-D(KLAKLAK)2, a peptide designed by Ellerby and coworkers (1999) (full sequence: ACDCRGDCFCGGKLAKLAKKLAKLAK), binds selectively to αVβ3 integrin receptors expressed in tumor neovasculature and, after internalization, effectively induces apoptosis of endothelial cells. The aim of this study was to examine if RGD-4C-GG-D(KLAKLAK)2 would efficiently target cells, among them B16(F10), that overexpress αVβ3 receptors, and whether it would be suitable for therapeutic treatment of primary B16(F10) murine melanoma tumors. Thus, the peptide would target two distinct tumor compartments: that formed by endothelium of blood vessels and that made up of neoplastic cells. The therapeutic peptide was recognized and did induce apoptosis in B16(F10) cell line. Tumor growth inhibition was observed following direct intratumoral administration. However, cessation of peptide administration led to rapid tumor growth and death of the animals.
Źródło:
Acta Biochimica Polonica; 2006, 53, 4; 801-805
0001-527X
Pojawia się w:
Acta Biochimica Polonica
Dostawca treści:
Biblioteka Nauki
Artykuł
Tytuł:
Fibronectin fragments in human seminal plasma.
Autorzy:
Kątnik-Prastowska, Iwona
Przybysz, Magdalena
Chełmońska-Soyta, Anna
Powiązania:
https://bibliotekanauki.pl/articles/1041450.pdf
Data publikacji:
2005
Wydawca:
Polskie Towarzystwo Biochemiczne
Tematy:
cellular domain of fibronectin
seminal plasma
fibronectin
Opis:
The study has revealed the presence of fibronectin (FN) fragments and a lack of intact FN in 72 seminal plasma samples. The FN fragmentation was examined by immunoblotting with a monoclonal antibody specific to the central cellular FN domain and was confirmed with a monoclonal antibody directed to the C-terminal domain of FN. Nine FN fragments between 60 and 200 kDa and five fragments of 60-150 kDa were identified in seminal plasma samples of normozoospermic and of terato-, oligoterato-, and oligoasthenoterato-spermic groups, respectively. The relative amounts of the 60, 90 and 100 kDa FN fragments were 2-3 times higher in seminal plasmas with abnormal semen characteristics than in the normozoospermic group. The results suggest that seminal plasma FN fragments may contribute to fertilization and the analysis of FN fragmentation may have a diagnostic value in andrological investigations.
Źródło:
Acta Biochimica Polonica; 2005, 52, 2; 557-560
0001-527X
Pojawia się w:
Acta Biochimica Polonica
Dostawca treści:
Biblioteka Nauki
Artykuł
Tytuł:
Bacterially expressed truncated F2 domain of Plasmodium falciparum EBA-140 antigen can bind to human erythrocytes
Autorzy:
Rydzak, Joanna
Kryńska, Katarzyna
Suchanowska, Anna
Kaczmarek, Radosław
Łukasiewicz, Jolanta
Czerwiński, Marcin
Jaśkiewicz, Ewa
Powiązania:
https://bibliotekanauki.pl/articles/1039687.pdf
Data publikacji:
2012
Wydawca:
Polskie Towarzystwo Biochemiczne
Tematy:
truncated F2 domain purification
human erythrocyte binding
EBA-140 antigen
Plasmodium falciparum
recombinant F2 domain expression
Opis:
The recently identified erythrocyte binding antigen-140 (EBA-140) is a member of the Plasmodium falciparum DBL family of erythrocyte binding proteins, which are considered as prospective candidates for malaria vaccine development. The EBA-140 ligand is a paralogue of the well-characterized P. falciparum EBA-175 antigen. They share homology of domain structure, including Region II, which consists of two homologous F1 and F2 domains and is responsible for ligand-erythrocyte interaction during invasion. It was shown that the F2 domain of EBA-175 antigen seems to be more important for erythrocyte binding. In order to study activity and immunogenicity of EBA-140 antigen F2 domain, it is necessary to obtain recombinant protein of high purity and in a sufficient amount, which used to pose a challenge due to the high content of disulphide bridges. Here, we present a new method for expression and purification of Plasmodium falciparum EBA-140 antigen F2 domain in E. coli Rosetta-gami strain in fusion with the maltose binding protein (MBP). The truncated F2 domain formed by spontaneous proteolytic degradation of the fusion protein was purified by affinity chromatography on Ni-NTA resin followed by size exclusion chromatography. Molecular mass of this protein was confirmed by mass spectrometry. Its N-terminal amino acid sequencing revealed a proteolytic cleavage site within the F2 domain. The proper folding of the recombinant, truncated F2 domain of EBA-140 antigen was confirmed by circular dichroism analysis. The truncated F2 domain can specifically bind to human erythrocytes but its binding is not as efficient as that of full Region II. This confirms that both the F1 and F2 domains of EBA-140 antigen are required for effective erythrocyte binding.
Źródło:
Acta Biochimica Polonica; 2012, 59, 4; 685-691
0001-527X
Pojawia się w:
Acta Biochimica Polonica
Dostawca treści:
Biblioteka Nauki
Artykuł
Tytuł:
Cloning and characterization of the yak gene coding for calpastatin and in silico analysis of its putative product
Autorzy:
Zhang, Liping
Ma, Binyun
Wu, Jianping
Fei, Chunhong
Yang, Lian
Wan, Hongling
Powiązania:
https://bibliotekanauki.pl/articles/1040417.pdf
Data publikacji:
2010
Wydawca:
Polskie Towarzystwo Biochemiczne
Tematy:
calpastatin
yak
domain
motif
functional site
calpaincalpastatin system
Opis:
The calcium-activated neutral proteases, μ- and m-calpain, along with their inhibitor, calpastatin, have been demonstrated to mediate a variety of Ca2+-dependent processes including signal transduction, cell proliferation, cell cycle progression, differentiation, apoptosis, membrane fusion, platelet activation and skeletal muscle protein degradation. The cDNA coding for yak calpastatin was amplified and cloned by RT-PCR to investigate and characterize the nucleotide/amino-acid sequence and to predict structure and function of the calpastatin. The present study suggests that the yak calpastatin gene encodes a protein of 786 amino acids that shares 99 % sequence identity with the amino-acid sequence of cattle calpastatin, and that the yak protein is composed of an N-terminal region (domains L and XL) and four repetitive homologous C-terminal domains (d1–d4), in which several prosite motifs are present including short peptide L54–64 (EVKPKEHTEPK in domain L) and GXXE/ DXTIPPXYR (in subdomain B), where X is a variable amino acid. Our results suggest the existence of other functional sites including potential phosphorylation sites for protein kinase C, cAMP- and cGMP-dependent protein kinase, casein kinase II, as well as N-myristoylation and amidation sites that play an important role in molecular regulation of the calpain/calpastatin system. The regulation of the calpain/calpastatin system is determined by the interaction between dIV and dVI in calpains and subdomains A, B, and C in calpastatin.
Źródło:
Acta Biochimica Polonica; 2010, 57, 1; 35-41
0001-527X
Pojawia się w:
Acta Biochimica Polonica
Dostawca treści:
Biblioteka Nauki
Artykuł
Tytuł:
Unexpected domain composition of MACC1 links MET signaling and apoptosis
Autorzy:
Kokoszyńska, Katarzyna
Kryński, Jacek
Rychlewski, Leszek
Wyrwicz, Lucjan
Powiązania:
https://bibliotekanauki.pl/articles/1040592.pdf
Data publikacji:
2009
Wydawca:
Polskie Towarzystwo Biochemiczne
Tematy:
protein structure modeling
colorectal cancer
bioinformatics
death domain
Opis:
Colorectal cancer, one of the most challenging malignancies, still has a limited number of recognized prognostic and predictive markers indicating appropriate treatment. MACC1 (metastasis-associated in colon cancer-1), a novel regulator of tumor growth and metastasis has recently been identified as an important prognostic factor of metastatic disease in colorectal cancer. The mechanism of MACC1 activity remains undetermined. Here we apply a combination of fold recognition and homology modeling algorithms to draft MACC1 function. The applied methods revealed that the MACC1 protein consists of four domains: ZU5, SH3, and two C-terminal death domains (DD). Previously a similar domain architecture (ZU5-DD) was observed in other proteins, involved mainly in signal transduction and apoptosis regulation. Based on the specific aspects of the closest homologues' biology functional hypotheses on MACC1 are proposed. A broad range of bioinformatic analyzes indicates that MACC1, besides its involvement in signal transduction from the MET receptor, links MET signaling and apoptosis.
Źródło:
Acta Biochimica Polonica; 2009, 56, 2; 317-324
0001-527X
Pojawia się w:
Acta Biochimica Polonica
Dostawca treści:
Biblioteka Nauki
Artykuł
Tytuł:
Degenerate specificity of PDZ domains from RhoA-specific nucleotide exchange factors PDZRhoGEF and LARG
Autorzy:
Smietana, Katarzyna
Kasztura, Monika
Paduch, Marcin
Derewenda, Urszula
Derewenda, Zygmunt
Otlewski, Jacek
Powiązania:
https://bibliotekanauki.pl/articles/1040739.pdf
Data publikacji:
2008
Wydawca:
Polskie Towarzystwo Biochemiczne
Tematy:
binding specificity
LARG
PDZ domain
PDZRhoGEF
phage display
Opis:
PDZ domains are ubiquitous protein-protein interaction modules which bind short, usually carboxyterminal fragments of receptors, other integral or membrane-associated proteins, and occasionally cytosolic proteins. Their role in organizing multiprotein complexes at the cellular membrane is crucial for many signaling pathways, but the rules defining their binding specificity are still poorly understood and do not readily explain the observed diversity of their known binding partners. Two homologous RhoA-specific, multidomain nucleotide exchange factors PDZRhoGEF and LARG contain PDZ domains which show a particularly broad recognition profile, as suggested by the identification of five diverse biological targets. To investigate the molecular roots of this phenomenon, we constructed a phage display library of random carboxyterminal hexapeptides. Peptide variants corresponding to the sequences identified in library selection were synthesized and their affinities for both PDZ domains were measured and compared with those of peptides derived from sequences of natural partners. Based on the analysis of the binding sequences identified for PDZRhoGEF, we propose a sequence for an 'optimal' binding partner. Our results support the hypothesis that PDZ-peptide interactions may be best understood when one considers the sum of entropic and dynamic effects for each peptide as a whole entity, rather than preferences for specific residues at a given position.
Źródło:
Acta Biochimica Polonica; 2008, 55, 2; 269-280
0001-527X
Pojawia się w:
Acta Biochimica Polonica
Dostawca treści:
Biblioteka Nauki
Artykuł
Tytuł:
A novel isoform of human lymphoid enhancer-binding factor-1 (LEF-1) gene transcript encodes a protein devoid of HMG domain and nuclear localization signal.
Autorzy:
Kobielak, Agnieszka
Kobielak, Krzysztof
Trzeciak, Wieslaw
Powiązania:
https://bibliotekanauki.pl/articles/1044190.pdf
Data publikacji:
2001
Wydawca:
Polskie Towarzystwo Biochemiczne
Tematy:
human LEF-1
novel transcript isoform
HMG domain
Opis:
Lymphoid enhancer-binding factor-1 (LEF-1), a member of the high mobility group (HMG) family of proteins, regulates expression of T-cell receptor-α gene and is one of the key regulatory molecules in the epithelial-mesenchymal interactions during embryonic development. Among others, LEF-1 regulates expression of cytokeratin genes involved in formation of hair follicles and the gene encoding the cell-adhesion molecule E-cadherin. Transcription factor LEF-1, which acts as a dimer, binds β-catenin and is involved in signal transduction by the wnt pathway. We have cloned and sequenced a novel isoform of human LEF-1 gene transcript. This isoform encodes a truncated protein devoid of HMG domain and nuclear localization signal but retaining β-catenin binding domain. This isoform might either act in a dominant-negative manner by interfering with native LEF-1, or might bind β-catenin in the cytosol, which would result in attenuation of the signals transmitted by theLEF-b-catenin pathway.
Źródło:
Acta Biochimica Polonica; 2001, 48, 1; 221-226
0001-527X
Pojawia się w:
Acta Biochimica Polonica
Dostawca treści:
Biblioteka Nauki
Artykuł
Tytuł:
GTP-binding properties of the membrane-bound form of porcine liver annexin VI.
Autorzy:
Kirilenko, Aneta
Golczak, Marcin
Pikuła, Sławomir
Bandorowicz-Pikuła, Joanna
Powiązania:
https://bibliotekanauki.pl/articles/1044028.pdf
Data publikacji:
2001
Wydawca:
Polskie Towarzystwo Biochemiczne
Tematy:
annexin VI
GTP-binding domain
TNP-GTP
circular dichroism
GTP binding
Opis:
Annexin VI (AnxVI) of molecular mass 68-70 kDa belongs to a multigenic family of ubiquitous Ca2+ - and phospholipid-binding proteins. In this report, we describe the GTP-binding properties of porcine liver AnxVI, determined with a fluorescent GTP analogue, 2'-(or 3')-O-(2,4,6-trinitrophenyl)guanosine 5'-triphosphate (TNP-GTP). The optimal binding of TNP-GTP to AnxVI was observed in the presence of Ca2+ and asolectin liposomes, as evidenced by a 5.5-fold increase of TNP-GTP fluorescence and a concomitant blue shift (by 17 nm) of its maximal emission wavelength. Titration of AnxVI with TNP-GTP resulted in the determination of the dissociation constant (Kd) and binding stoichiometry that amounted to 1.3 μM and 1:1 TNP-GTP/AnxVI, mole/mole, respectively. In addition, the intrinsic fluorescence of the membrane-bound form of AnxVI was quenched by TNP-GTP and this was accompanied by fluorescence resonance energy transfer (FRET) from AnxVI Trp residues to TNP-GTP. This indicates that the GTP-binding site within the AnxVI molecule is probably located in the vicinity of a Trp-containing domain of the protein. By controlled proteolysis of human recombinant AnxVI, followed by purification of the proteolytic fragments by affinity chromatography on GTP-agarose, we isolated a 35 kDa fragment corresponding to the N-terminal half of AnxVI containing Trp192. On the basis of these results, we suggest that AnxVI is a GTP-binding protein and the binding of the nucleotide may have a regulatory impact on the interaction of annexin with membranes, e.g. formation of ion channels by the protein.
Źródło:
Acta Biochimica Polonica; 2001, 48, 4; 851-865
0001-527X
Pojawia się w:
Acta Biochimica Polonica
Dostawca treści:
Biblioteka Nauki
Artykuł
Tytuł:
3D Domain swapping, protein oligomerization, and amyloid formation.
Autorzy:
Jaskólski, Mariusz
Powiązania:
https://bibliotekanauki.pl/articles/1043850.pdf
Data publikacji:
2001
Wydawca:
Polskie Towarzystwo Biochemiczne
Tematy:
protein aggregation
amyloid
amyloid fibrils
3D domain swapping
conformational diseases
amyloidosis
Opis:
In 3D domain swapping, first described by Eisenberg, a structural element of a monomeric protein is replaced by the same element from another subunit. This process requires partial unfolding of the closed monomers that is then followed by adhesion and reconstruction of the original fold but from elements contributed by different subunits. If the interactions are reciprocal, a closed-ended dimer will be formed, but the same phenomenon has been suggested as a mechanism for the formation of open-ended polymers as well, such as those believed to exist in amyloid fibrils. There has been a rapid progress in the study of 3D domain swapping. Oligomers higher than dimers have been found, the monomer-dimer equilibrium could be controlled by mutations in the hinge element of the chain, a single protein has been shown to form more than one domain-swapped structure, and recently, the possibility of simultaneous exchange of two structural domains by a single molecule has been demonstrated. This last discovery has an important bearing on the possibility that 3D domain swapping might be indeed an amyloidogenic mechanism. Along the same lines is the discovery that a protein of proven amyloidogenic properties, human cystatin C, is capable of 3D domain swapping that leads to oligomerization. The structure of do-main-swapped human cystatin C dimers explains why a naturally occurring mutant of this protein has a much higher propensity for aggregation, and also suggests how this same mechanism of 3D domain swapping could lead to an open-ended polymer that would be consistent with the cross-β structure, which is believed to be at the heart of the molecular architecture of amyloid fibrils.
Źródło:
Acta Biochimica Polonica; 2001, 48, 4; 807-827
0001-527X
Pojawia się w:
Acta Biochimica Polonica
Dostawca treści:
Biblioteka Nauki
Artykuł
Tytuł:
Hemagglutinin stalk domain from H5N1 strain as a potentially universal antigen
Autorzy:
Uranowska, Karolina
Tyborowska, Jolanta
Jurek, Anna
Szewczyk, Bogusław
Gromadzka, Beata
Powiązania:
https://bibliotekanauki.pl/articles/1039261.pdf
Data publikacji:
2014
Wydawca:
Polskie Towarzystwo Biochemiczne
Tematy:
H5N1
universal influenza antigen
hemagglutinin stalk domain
universal influenza antibodies
FI6
Opis:
Influenza A virus infections are the major public health concern and cause significant morbidity and mortality each year worldwide. Vaccination is the main strategy of influenza epidemic prevention. However, seasonal vaccines induce strain-specific immunity and must be reformulated annually based on prediction of the strains that will circulate in the next season. Thus, it is essential to develop vaccines that would induce broad and persistent immunity to influenza viruses. Hemagglutinin is the major surface antigen of the influenza virus. Recent studies revealed the importance of HA stalk-specific antibodies in neutralization of different influenza virus strains. Therefore, it is important to design an immunogen that would focus the immune response on the HA stalk domain in order to elicit neutralizing antibodies. In the present study, we report characterization of a conserved truncated protein, potentially a universal influenza virus antigen from the H5N1 Highly Pathogenic Avian Influenza A virus strain. Our results indicate that exposure of the HA stalk domain containing conserved epitopes results in cross reactivity with different antibodies (against group 1 and 2 HAs). Additionally, we conclude that HA stalk domain contains not only conformational epitopes recognized by universal FI6 antibody, but also linear epitopes recognized by other antibodies.
Źródło:
Acta Biochimica Polonica; 2014, 61, 3; 541-550
0001-527X
Pojawia się w:
Acta Biochimica Polonica
Dostawca treści:
Biblioteka Nauki
Artykuł
Tytuł:
Cloning and expression of a new recombinant thrombolytic and anthithrombotic agent - a staphylokinase variant
Autorzy:
Kowalski, Michał
Brown, George
Bieniasz, Magdalena
Oszajca, Katarzyna
Chabielska, Ewa
Pietras, Tadeusz
Szemraj, Zofia
Makandjou-Ola, Eusebio
Bartkowiak, Jacek
Szemraj, Janusz
Powiązania:
https://bibliotekanauki.pl/articles/1040615.pdf
Data publikacji:
2009
Wydawca:
Polskie Towarzystwo Biochemiczne
Tematy:
K2 domain of t-PA
thrombolytic and antithrombotic agents
thrombolysis
staphylokinase
recombinant protein
hirulog
antiplatelet activity
Opis:
To develop a more potent antithrombin agent with thrombolytic and antiplatelet properties, a new staphylokinase (SAK) variant was constructed. The kringle 2 domain (K2) of tissue type-plasminogen activator (t-PA) containing a fibrin-specific binding site (i), the RGD sequence (Arg-Gly-Asp) for the prevention of platelet aggregation (ii) and the antithrombotic agent - hirulog (iii) was assembled to the C-terminal part of recombinant staphylokinase (r-SAK). cDNA for the hybrid protein SAK-RGD-K2-Hirul was cloned into Pichia pastoris pPIC9K yeast expression vector. The introduction of K2 t-PA, the RGD sequence and hirulog into the C-terminus of r-SAK did not alter the staphylokinase activity. We observed a higher clot lysis potency of SAK-RGD-K2-Hirul as evidenced by a faster and more profound lysis of 125I-labeled human fibrin clots. The potency of thrombin inhibition by the hirulog C-terminal part of the recombinant fusion protein was almost identical to that of r-Hir alone. These results suggest that the SAK-RGD-K2-Hirul construct can be a more potent and faster-acting thrombolytic agent with better antithrombin and antiplatelet properties compared to r-SAK and SAK-RGD-K2-Hir.
Źródło:
Acta Biochimica Polonica; 2009, 56, 1; 41-53
0001-527X
Pojawia się w:
Acta Biochimica Polonica
Dostawca treści:
Biblioteka Nauki
Artykuł

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