نتایج جستجو برای: پروتیین ha2

تعداد نتایج: 1474  

ژورنال: :مجله دانشکده پزشکی دانشگاه علوم پزشکی تهران 0
سمیه زمانی somayeh zamani department of biology, science and research branch, islamic azad university, tehran, iran.گروه زیست شناسی، دانشگاه آزاد اسلامی واحد علوم و تحقیقات، تهران فاطمه فتوحی چاهوکی fatemeh fotouhi chahouki department of virology, influenza research lab, pasteur institute of iran, tehran, iran.گروه ویروس شناسی، انستیتو پاستور ایران زهرا نورمحمدی zahra nourmohammadi department of biology, science and research branch, islamic azad university, tehran, iran.گروه زیست شناسی، دانشگاه آزاد اسلامی واحد علوم و تحقیقات، تهران سعیده صادقی نشاط saeideh sadeghi neshat department of virology, influenza research lab, pasteur institute of iran, tehran, iran.گروه ویروس شناسی، انستیتو پاستور ایران وحیده مظاهری vahideh mazaheri department of virology, influenza research lab, pasteur institute of iran, tehran, iran.گروه ویروس شناسی، انستیتو پاستور ایران علی ترابی ali torabi department of virology, influenza research lab, pasteur institute of iran, tehran, iran.گروه ویروس شناسی، انستیتو پاستور ایران بهرخ فرهمند

زمینه و هدف: ویروس آنفلوآنزا یکی از عوامل مرگ ومیر بالا در جهان است. پژوهشگران به استفاده از آنتی ژن های حفاظت شده این ویروس (مانند زیرواحد کوچک مولکول گلیکوپروتیین هماگلوتینین) به منظور ساخت واکسن و پژوهش های سرولوژیک توجه خاص دارند. این پژوهش با هدف تولید آنتی بادی های پلی کلونال علیه ha2 با کارایی لازم اجرا شد. روش بررسی: این پژوهش از نوع علوم پایه (در زمینه تولید فرآورده) بود و از مهر 1392 ...

ترابی, علی , زمانی, سمیه , صادقی نشاط, سعیده , فتوحی چاهوکی, فاطمه , فرهمند, بهرخ , مظاهری, وحیده , نورمحمدی, زهرا ,

Background: The influenza virus is one of the most important factors for higher morbidity and mortality in the world. Recently, researchers have been focused on influenza conserved antigenic proteins such as hemagglutinin stalk domain (HA2) for vaccine production and serological studies. The HA2 plays a major role in the fusion of the virus with host cells membrane. The immunity system enables ...

Journal: :Virus research 2006
Yingchao Nie Qian Wang Changyong Liang Minggang Fang Zehua Yu Xinwen Chen

The open reading frame 2 (ha2) of the Helicoverpa armigera single nucleocapsid nucleopolyhedrovirus (HaSNPV), a conserved gene in most baculoviruses from lepidopteran insects such as p78/83 of the Autographa californica MNPV, was characterized. It is 1,242 bp long and potentially encodes a 45.9 kDa. Ha2 is conserved among baculoviruses from lepidopteran insects. Ha2 transcripts were detected fr...

Journal: :Journal of virology 2008
Qian Wang Yun Wang Changyong Liang Jianhua Song Xinwen Chen

The HA2 protein of the Helicoverpa armigera single-nucleocapsid nucleopolyhedrovirus (HearNPV) is a WASP homology protein capable of nucleating branched actin filaments in the presence of the Arp2/3 complex in vitro. To determine the role of ha2 in the HearNPV life cycle, ha2 knockout and ha2 repair bacmids were constructed. Transfection and infection analysis demonstrated that the ha2 null bac...

Journal: :The Journal of biological chemistry 2011
Chang Sup Kim Raquel F Epand Eugenia Leikina Richard M Epand Leonid V Chernomordik

One of the best characterized fusion proteins, the influenza virus hemagglutinin (HA), mediates fusion between the viral envelope and the endosomal membrane during viral entry into the cell. In the initial conformation of HA, its fusogenic subunit, the transmembrane protein HA2, is locked in a metastable conformation by the receptor-binding HA1 subunit of HA. Acidification in the endosome trigg...

2012
Zuzana Staneková Vojtech Mucha Tatiana Sládková Hana Blaškovičová František Kostolanský Eva Varečková

BACKGROUND The conserved, fusion-active HA2 glycopolypeptide (HA2) subunit of influenza A hemagglutinin comprises four distinct antigenic sites. Monoclonal antibodies (MAbs) recognizing three of these sites are broadly cross-reactive and protective. OBJECTIVES This study aimed to establish whether antibodies specific to these three antigenic sites were elicited during a natural influenza infe...

Journal: :Proceedings of the National Academy of Sciences of the United States of America 1995
J Chen S A Wharton W Weissenhorn L J Calder F M Hughson J J Skehel D C Wiley

The extensive refolding of the membrane-anchoring chain of hemagglutinin (HA) of influenza virus (termed HA2) in cellular endosomes, which initiates viral entry by membrane fusion, suggests that viral HA is meta-stable. HA2 polypeptide residues 38-175 expressed in Escherichia coli are reported here to fold in vivo into a soluble trimer. The structure appears to be the same as the low-pH-induced...

Journal: :Peptides 2012
Ji-Sing Liou Betty Revon Liu Adam L Martin Yue-Wern Huang Huey-Jenn Chiang Han-Jung Lee

Endocytosis has been proposed as one of the primary mechanisms for cellular entry of cell-penetrating peptides (CPPs) and their cargoes. However, a major limitation of endocytic pathway is entrapment of the CPP-cargo in intracellular vesicles from which the cargo must escape into the cytoplasm to exert its biological activity. Here we demonstrate that a CPP tagged with an endosomolytic fusion p...

Journal: :Advanced pharmaceutical bulletin 2015
Ali Ameghi Behzad Baradaran Khosrow Aghaiypour Abolfazl Barzegar Yones Pilehvar-Soltanahmadi Masood Moghadampour Morteza Taghizadeh Nosratollah Zarghami

PURPOSE The purpose was to design a new construction containing influenza virus (H1N1) M2e gene and HA2 gene by bioinformatics approach, cloning the construct in to Escherichia coli and produce M2e-HA2 peptide. METHODS The procedure was done by virus cultivation in SPF eggs, hemagglutination assay (HA), RNA isolation, RT-PCR, primers designed (DNAMAN 4 and Oligo7), virtual fusion construction...

Journal: :Bioscience reports 1992
T Korte K Ludwig A Herrmann

The hydropathy profile of hemagglutinin (HA) subunits HA1 and HA2 of influenza virus X31 and A/PR 8/34 is analyzed at different pH. At neutral pH (7.4) pronounced hydrophobic sequences of HA correspond to the N-terminus and the transmembrane spanning sequence of HA2. At pH 5.0 where influenza virus is known to fuse with biological membranes several hydrophobic sequences in the ectodomain exist ...

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