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Identification and characterization of the hemoglobin‐binding domain of hemoglobin receptor in Leishmania
Author(s) -
Rastogi Ruchir,
Verma Jitender Kumar,
Singh Vijay,
Krishnamurthy Ganga,
Sood Chandni,
Kapoor Anjali,
Kumar Kamal,
Ansari Irshad,
Mukhopadhyay Amitabha
Publication year - 2021
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1002/1873-3468.14027
Subject(s) - amastigote , hemoglobin , leishmania , peptide , chemistry , receptor , biochemistry , biology , parasite hosting , world wide web , computer science
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 .