نتایج جستجو برای: core binding domain of HMW1
تعداد نتایج: 21232325 فیلتر نتایج به سال:
colonization of nontypeable haemophilus influenzae (nthi) in nasopharynx causes respiratory tract disease. in 80% of clinical isolates, hmw proteins are the major adhesions and induce protective antibodies in the hosts. therefore, it can be used as a vaccine candidate. the aim of this study is designing and cloning of the conserved regions of nthi hmw1 core binding domain.in this study, the sta...
Colonization of nontypeable Haemophilus influenzae (NTHi) in nasopharynx causes respiratory tract disease. In 80% of clinical isolates, HMW proteins are the major adhesions and induce protective antibodies in the hosts. Therefore, it can be used as a vaccine candidate. The aim of this study is designing and cloning of the conserved regions of NTHi hmw1 core binding domain.In this study, the sta...
The cytoskeletal proteins HMW1 and HMW2 are components of the terminal organelle of the cell wall-less bacterium Mycoplasma pneumoniae. HMW1 is required for a tapered, filamentous morphology but exhibits accelerated turnover in the absence of HMW2. Here, we report that a reciprocal dependency exists between HMW1 and HMW2, with HMW2 subject to accelerated turnover with the loss of HMW1. Furtherm...
Cytadherence proteins of Mycoplasma pneumoniae are localized at the attachment organelle, which is involved in adhesion, gliding motility, and cell division. The localization of these proteins in cytadherence-deficient mutants was examined by immunofluorescence microscopy. In the class I-2 mutant, which has a frameshift mutation in the hmw2 gene, fluorescent foci for HMW1 and HMW3 were found wi...
Nontypeable Haemophilus influenzae (NTHi) is a common cause of localized respiratory tract disease and initiates infection by colonizing the nasopharynx. Approximately 75 to 80% of NTHi clinical isolates produce proteins that belong to the HMW family of adhesins, which are believed to facilitate colonization. The prototype HMW adhesins are designated HMW1 and HMW2 and were identified in NTHi st...
The HMW1 and HMW2 adhesins of nontypeable Haemophilus influenzae are high-molecular weight proteins that are secreted by the two-partner secretion (TPS) pathway, also known as the Type Vb secretion pathway [1,2]. TPS systems typically consist of a large extracellular protein called a TpsA protein (encoded by a tpsA gene) and a cognate outer membrane pore-forming translocator protein called a Tp...
The Haemophilus influenzae HMW1 adhesin is an important virulence exoprotein that is secreted via the two-partner secretion pathway and is glycosylated at multiple asparagine residues in consensus N-linked sequons. Unlike the heavily branched glycans found in eukaryotic N-linked glycoproteins, the modifying glycan structures in HMW1 are mono-hexoses or di-hexoses. Recent work demonstrated that ...
The genomic sequence of Mycoplasma pneumoniae establish this cell-wall-less prokaryote as among the smallest known microorganisms capable of self-replication. However, this genomic simplicity and corresponding biosynthetic austerity are sharply contrasted by the complex terminal structure found in this species. This tip structure (attachment organelle) directs colonization of the human respirat...
we have two part in this thesis, at first: the interaction of native calf thymus dna (ct-dna) with two anthraquinones including quinizarin (1,4- dihydroxy anthraquinone) and danthron (1,8- dihydroxy anthraquinone) in a mixture of 0.04 m brittone-robinson buffer and 50% of ethanol were studied at physiological ph by uv-vis absorption, florescence, circular dichroism spectroscopic methods, viscos...
some new water-soluble schiff base complexes of na2[m(5-so3-1,2-salophen)].nh2o; (5-so3-1,2-salophen = n,n’-bis(5-sulphosalicyliden)-1,2-phenylendiamine); na2[m(5-so3-2,3-salpyr)(h2o)n].2h2o; (5-so3-2,3-salpyr = n,n’-bis(5-sulphosalicyliden)-2,3-diaminopyridine); and na2[m(5-so3-3,4-salbenz)(h2o)n].nh2o; (5-so3-3,4-salbenz = n,n’-bis(5-sulphosalicyliden)-3,4-diaminobenzophenon); where m = cu, n...
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