The C-terminal 32-mer fragment of hemoglobin alpha is an amyloidogenic peptide with antimicrobial properties.
Cell Mol Life Sci
; 80(6): 151, 2023 May 17.
Article
in English
| MEDLINE | ID: covidwho-2325328
ABSTRACT
Antimicrobial peptides (AMPs) are major components of the innate immune defense. Accumulating evidence suggests that the antibacterial activity of many AMPs is dependent on the formation of amyloid-like fibrils. To identify novel fibril forming AMPs, we generated a spleen-derived peptide library and screened it for the presence of amyloidogenic peptides. This approach led to the identification of a C-terminal 32-mer fragment of alpha-hemoglobin, termed HBA(111-142). The non-fibrillar peptide has membranolytic activity against various bacterial species, while the HBA(111-142) fibrils aggregated bacteria to promote their phagocytotic clearance. Further, HBA(111-142) fibrils selectively inhibited measles and herpes viruses (HSV-1, HSV-2, HCMV), but not SARS-CoV-2, ZIKV and IAV. HBA(111-142) is released from its precursor by ubiquitous aspartic proteases under acidic conditions characteristic at sites of infection and inflammation. Thus, HBA(111-142) is an amyloidogenic AMP that may specifically be generated from a highly abundant precursor during bacterial or viral infection and may play an important role in innate antimicrobial immune responses.
Keywords
Full text:
Available
Collection:
International databases
Database:
MEDLINE
Main subject:
Zika Virus
/
Zika Virus Infection
/
COVID-19
Type of study:
Prognostic study
Limits:
Humans
Language:
English
Journal:
Cell Mol Life Sci
Journal subject:
Molecular Biology
Year:
2023
Document Type:
Article
Affiliation country:
S00018-023-04795-8
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