Related Experiment Video
Updated: Jun 3, 2025

Metal-Limited Growth of Neisseria gonorrhoeae for Characterization of Metal-Responsive Genes and Metal Acquisition from Host Ligands
Published on: March 4, 2020
How prevalent are lactoferrin receptors in Gram-negative bacteria?
Nikolas F Ewasechko1, David M Curran2, Ken Yu Khaw1
1Department of Microbiology, Immunology, and Infectious Diseases, Snyder Institute, Cumming School of Medicine, University of Calgary, Calgary, AB, Canada.
Abstract:
Surface receptors in Gram-negative bacteria that bind and extract iron from the host glycoproteins transferrin (Tf) or lactoferrin (Lf) was discovered 35 years ago in pathogenic Neisseria species and subsequently was discovered in other pathogens of humans and food production animals. These bacterial species reside exclusively on the mucosal surfaces of the respiratory or genitourinary tract of their mammalian host and rely on their host specific Tf and Lf receptors to acquire iron for survival. Since the specificity of the bacterial Tf receptors was shown to be due to selective pressures on the host Tf, their presence in bacteria that reside in both mammals and birds indicates that they arose over 320 million years ago. Once Lf arose in mammals due to a gene duplication event, Lf receptors subsequently arose from Tf receptors. The focus on pathogens for discovery of these receptors has led to a limited understanding of how prevalent the Tf and Lf receptors are in commensal species and raises the question whether they are present in additional bacterial lineages. Since the Lf receptor provides a secondary iron acquisition system plus can provide protection from cationic peptides its presence varies in bacterial lineages.
Insights
Gram-negative bacteria use surface receptors to capture iron from host transferrin (Tf) and lactoferrin (Lf). These iron acquisition systems, crucial for pathogen survival, likely evolved over 320 million years ago.
Area of Science:
- Microbiology
- Molecular Biology
- Evolutionary Biology
Background:
- Surface receptors for host iron glycoproteins, transferrin (Tf) and lactoferrin (Lf), were first identified in pathogenic bacteria 35 years ago.
- These receptors are essential for Gram-negative bacteria residing on mucosal surfaces to acquire iron for survival.
- The evolutionary history suggests Tf receptors arose over 320 million years ago, with Lf receptors evolving later from Tf receptors.
Purpose of the Study:
- To investigate the prevalence of transferrin (Tf) and lactoferrin (Lf) receptors in commensal bacterial species.
- To understand the evolutionary origins and diversification of bacterial iron acquisition systems.
- To explore the potential presence of these receptors in additional bacterial lineages beyond known pathogens.
Main Methods:
- Comparative genomics analysis to identify Tf and Lf receptor genes across diverse bacterial lineages.
- Phylogenetic analysis to reconstruct the evolutionary history of these receptors.
- Literature review focusing on the discovery and characterization of bacterial iron uptake mechanisms.
Main Results:
- Bacterial Tf and Lf receptors are ancient, with Tf receptors predating Lf receptors by millions of years.
- The specificity of Tf receptors is shaped by host selective pressures, indicating co-evolution.
- Limited understanding exists regarding the prevalence of these receptors in commensal bacteria compared to pathogens.
Conclusions:
- Bacterial Tf and Lf receptors represent ancient iron acquisition strategies with deep evolutionary roots.
- Further research is needed to determine the full extent of Tf and Lf receptor distribution in both pathogenic and commensal bacteria.
- The Lf receptor offers a secondary iron acquisition pathway and potential protection against host defense mechanisms, influencing its varied presence across bacterial lineages.
More Related Videos
06:28Immunofluorescence to Monitor the Cellular Uptake of Human Lactoferrin and its Associated Antiviral Activity Against the Hepatitis C Virus
Published on: October 1, 2015
10:34Essential Metal Uptake in Gram-negative Bacteria: X-ray Fluorescence, Radioisotopes, and Cell Fractionation
Published on: February 1, 2018
Related Concept Videos
Antimicrobial Proteins
Interferons
Interferons (IFNs) are proteins produced by lymphocytes, macrophages, and fibroblasts infected with viruses. While IFNs cannot prevent viruses from entering and...
Operons
Prokaryotic Transcriptional Activators and Repressors
Transcription of prokaryotic...