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

FEBS Letters

article

Ruchir Rastogi¹  Jitender Kumar Verma²  Vijay Singh¹  Ganga Krishnamurthy¹  Chandni Sood²  Anjali Kapoor²  Kamal Kumar²  Irshad Ansari¹  Amitabha Mukhopadhyay² 

[1] National Institute of Immunology;Kusuma School of Biological Sciences, Indian Institute of Technology

关键词: domain;    endocytosis;    hemoglobin;    Leishmania;    receptor;   

DOI  :  10.1002/1873-3468.14027

来源: John Wiley & Sons Ltd.

【 摘 要 】

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 .

【 授权许可】

Unknown