Identification and characterization of the hemoglobin-binding domain of hemoglobin receptor in Leishmania.

IF 3 4区生物学 Q3 BIOCHEMISTRY & MOLECULAR BIOLOGY FEBS Letters Pub Date : 2021-02-01 Epub Date: 2021-01-02 DOI:10.1002/1873-3468.14027

Ruchir Rastogi, Jitender Kumar Verma, Vijay Singh, Ganga Krishnamurthy, Chandni Sood, Anjali Kapoor, Kamal Kumar, Irshad Ansari, Amitabha Mukhopadhyay

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引用次数: 3

Abstract

Leishmania internalize hemoglobin (Hb) via a specific receptor (HbR) for their survival. To identify the Hb-binding domain of HbR, we cloned and expressed several truncated proteins of HbR and determined their ability to bind Hb. Our findings reveal that 90% of Hb-binding activity is retained in HbR^41-80 in comparison with HbR^1-471 . We synthesized a 40 amino acid peptide (SSEKMKQLTMYMIHEMVEGLEGRPSTVRMLPSFVYTSDPA) corresponding to HbR^41-80 and found that it specifically binds Hb. Subsequently, we found that the HbR^41-80 peptide completely blocks Hb uptake in both promastigote and amastigote forms of Leishmania and, thereby, inhibits the growth of the parasite. These results demonstrate that HbR^41-80 is the Hb-binding domain of HbR, which might be used as a potential therapeutic agent to inhibit the growth of Leishmania.

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利什曼原虫血红蛋白受体血红蛋白结合区域的鉴定与表征。

利什曼原虫通过特定受体(HbR)内化血红蛋白(Hb)以维持生存。为了确定HbR的Hb结合结构域，我们克隆并表达了几个HbR的截断蛋白，并确定了它们与Hb的结合能力。我们的研究结果显示，与HbR1-471相比，HbR41-80中保留了90%的hb结合活性。我们合成了一个与HbR41-80对应的40个氨基酸的肽(SSEKMKQLTMYMIHEMVEGLEGRPSTVRMLPSFVYTSDPA)，发现它特异性结合Hb。随后，我们发现HbR41-80肽完全阻断利什曼原虫promastigote和amastigote形式的Hb摄取，从而抑制寄生虫的生长。这些结果表明，HbR41-80是HbR的hb结合结构域，可能作为抑制利什曼原虫生长的潜在治疗剂。

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来源期刊

FEBS Letters 生物-生化与分子生物学

CiteScore

6.60

自引率

2.90%

发文量

303

审稿时长

1 months

期刊介绍： FEBS Letters is one of the world''s leading journals in molecular biology and is renowned both for its quality of content and speed of production. Bringing together the most important developments in the molecular biosciences, FEBS Letters provides an international forum for Minireviews, Research Letters and Hypotheses that merit urgent publication.