鬼鬼 發問時間: 社會與文化語言 · 6 年前

英文文章翻譯~~(求助)

Researchers at Rutgers University and the University of Texas at Austin have reported a discovery that could help scientists develop drugs to fight seasonal influenza epidemics caused by the common influenza B strain.

Their discovery also helps explain how influenza B is limited to humans, and why it cannot be as virulent as A strains that incorporate new genes from influenza viruses that infect other species. The devastating flu pandemic of 1918, the pandemics of 1968 and 1977, and the avian influenza that emerged in the middle of the last decade were caused by influenza A viruses. Understanding features of influenza B virus that limit it to humans will help scientists better understand how influenza A strains are able to cross species.

The researchers have determined the three-dimensional structure of a complex between an influenza B virus protein and one of its human protein targets, resulting in suppression of the cell's natural defenses to the infection and paving the way for the virus to replicate efficiently.

Their findings are detailed in a paper published in the most recent issue of PNAS (Proceedings of the US National Academy of Sciences).

"Our study shows the basis by which non-structural protein 1 of influenza B, or NS1B, binds to a human host protein, immobilizing it to prevent it from fighting the virus," said Gaetano Montelione, a lead author and professor of biochemistry and molecular biology, School of Arts and Sciences, at Rutgers. That human protein, known as interferon-stimulated gene 15 protein or ISG15, is an essential part of the defense mechanism that human cells use to protect themselves from viral infections. Chemicals that block the binding of NS1B to ISG15 may have antiviral potential against influenza B virus.

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The study, led by professors Montelione and Robert Krug at the University of Texas at Austin, also reveals why NS1B cannot bind ISG15 molecules in other species, such as dogs or mice.

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Only human and non-human primate ISG15 proteins have a unique molecular sequence in a small part of the protein that makes it possible to bind to the NS1B protein. So far, influenza B virus has been found only in humans.

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"The three-dimensional structure of the NS1B-ISG15 complex, which we determined

using X-ray crystallography, has given us a clear understanding of the molecular basis

for this species specificity," said Krug, professor and chair of molecular genetics and

microbiology.

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"Flu infections continue to be a major health problem, with more effective drugs

critically needed to treat infected individuals and control potential pandemics," said

Aaron Shatkin, director of the Center for Advanced Biotechnology and Medicine

(CABM) at Rutgers and an eminent virologist.

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"This discovery opens new

possibilities for achieving these very important goals."

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Participating in the study from Rutgers were Rongjin Guan, Li-Ching Ma and

Brendan Amer, who along with Montelione are members of CABM and the Northeast

Structural Genomics Consortium.

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They were joined by Paul Leonard of the Robert

Wood Johnson Medical School, University of Medicine and Dentistry of New Jersey,

who is also a member of CABM and the Howard Hughes Medical Institute.

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Participating from the University of Texas at Austin were Haripriya Sridharan and

Chen Zhao, who along with Krug are also members of the university's Institute for

Cellular and Molecular Biology.

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The work was supported by grants from the Protein Structure Initiative (PSI-Biology)

Program of the National Institutes of Health and its National Institute of General

Medical Sciences, the National Institute of Allergy and Infectious Disease, and the

Howard Hughes Medical Institute.

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Three-dimensional structure of a complex between influenza B virus protein, NS1B, represented as the solid form, and the human protein that fights infections, ISG15, represented as pink and magenta ribbons and strands.

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The sequence of the ISG15 protein found only in humans and non-human primates, represented as a short dark blue strand, binds to the NS1B protein, immobilizing ISG15 and preventing it from fighting the virus. Researchers determined the structure using X-ray crystallography.

2 個解答

評分
  • 6 年前
    最佳解答

    研究人員在羅格斯大學和德州大學奧斯汀分校報告了這一發現可能幫助科學家開發出藥物來對抗引起的常見的乙型流感株季節性流感流行。

    他們的發現也有助於解釋乙型流感是如何限於人類,為什麼就不能像有毒的A毒株,納入新基因的流感病毒感染其他物種。 1918年的毀滅性的流感大流行,1968年和1977年的大流行,以及禽流感,在過去十年中出現了由甲型流感病毒引起的了。了解B型流感病毒的功能,限制它給人類將幫助科學家更好地了解流感毒株如何能夠跨越物種。

    研究人員已經確定了B型流感病毒的蛋白質和其人力蛋白質目標之一,導致抑制細胞的天然防禦能力,以感染和鋪平了道路病毒複製效率之間的複雜的三維結構。

    他們的研究結果詳見刊登在最近的美國國家科學院院刊(科學美國國家科學院院刊)問題的文件。

    “我們的研究表明基礎由乙型流感的非結構蛋白1,或NS1B,結合到人類宿主蛋白,使其無法移動,以防止它從對抗病毒,”加埃塔諾Montelione,主要作者和生物化學教授說:分子生物學,學校的藝術和科學,在羅格斯大學。人類蛋白質,被稱為干擾素刺激基因15蛋白或ISG15,是人體細胞利用,以保護自己免受病毒感染的防禦機制的重要組成部分。化學物質,阻止NS1B對ISG15的結合可能對B型流感病毒的抗病毒的潛力。

    該研究由教授Montelione和羅伯特克魯格在得克薩斯大學奧斯汀分校,也揭示了為什麼NS1B不能綁定ISG15分子在其他物種,如狗或老鼠。

    只有人類和非人類靈長類動物ISG15蛋白具有在,使得它可以綁定到NS1B蛋白的蛋白質的一小部分,一個獨特的分子序列。到目前為止,乙型流感病毒已被發現,只有在人類。

    該NS1B-ISG15絡合物“的三維結構,這是我們確定利用X射線晶體學,已經給我們的分子基礎有清晰的認識這個種屬特異性,說:“克魯格教授和分子遺傳學的椅子上,微生物學。

    “流感感染仍然是一個主要的健康問題,以更有效的藥物急需治療感染的個體和控制潛在的流行病" 亞倫Shatkin說,該中心的先進生物技術和醫學主任(CABM)在Rutgers和一個著名的病毒學家。

    “這一發現開闢了新的準備為實現這些非常重要的目標“。

    在研究中從羅格斯大學參加了晉官,李菁和馬布倫丹·阿米爾,他們是Montelione是CABM成員和東北結構基因組學聯盟。

    他們是由羅伯特·保羅·倫納德也加入Wood Johnson醫學院,新澤西醫學與牙科大學,誰也CABM的成員和霍華德休斯醫學研究所。

    從得克薩斯大學奧斯汀分校參加了Haripriya Sridharan和陳釗,誰與克魯格也是大學的研究所成員細胞與分子生物學。

    這項工作是由來自蛋白質結構倡議(PSI-生物)資助項目健康與一般其研究所國家機構的計劃醫學,過敏和傳染病國家研究所和霍華德休斯醫學研究所。

    B型流感病毒蛋白,NS1B,表示為固體形式,並且打架感染,ISG15,表示為粉紅色和品紅色色帶和股線的人蛋白質之間的複合物的三維結構。

    只發現​​於人類和非人類靈長類動物的ISG15蛋白的序列,表示為一個短的深藍色鏈,結合到NS1B蛋白質,ISG15固定,防止它從對抗病毒。研究人員使用X-射線晶體學測定的結構。

    參考資料: google翻釋
  • 6 年前

    這麼一大篇文章 請人翻譯

    然後只給5點

    你覺得這種投資報酬率成正比 也ok啦 ^^

    我可以確定 不會有人想理會你

    除非你喜歡google翻譯的版本啦

    所以建議你把問題給砍了吧

    人家電影字幕 翻譯一個字 好歹也有錢賺

    就算不是算字 也有算分鐘的

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