Recombinant Human Lactoferrin: An Opportunity to Treat the Neonatal and Adult Severe Sepsis

Karel Petrak*

Recombinant Human Lactoferrin: An Opportunity to Treat the Neonatal and Adult Severe Sepsis

Human lactoferrin has been described by Kowalczyk etal as a “miracle molecule”.

Their justification for such an accolade is that lactoferrin acts against oxidative stress
damage and has a range of beneficial activities such as anti-pathogenic,
anti-cancer, anti-inflammatory, immunomodulatory, and deoxyribonucleic acid -regulatory
that play a role in health and pathology throughout life.

hLF is an iron-binding glycoprotein and the second most abundant protein
in human milk.

It is found on mucosal surfaces and in mature human milk, tears, saliva, seminal fluid,
and secondary granules of neutrophils and in many body fluids such as mucosal secretions,
including tears, saliva, vaginal fluids, semen, nasal and bronchial secretions, bile, gastrointestinal
fluids, and urine, and bodily fluids such as blood plasma and amniotic fluid.

In addition, the expression and secretion of hLF on mucosal surfaces and its release
at inflammatory sites have established its role as an agent of innate immunity.

hLF could be an attractive synergistic agent with antifungals and probiotics.
Bovine LF has been investigated extensively. It inhibits the growth of various bacteria, fungi,
viruses, and parasites.

A high homology between human and bovine LFs suggests that both forms may provide
similar health benefits. hLF is glycosylated with highly branched complex/hybrid
type N-glycans, mainly sialylated and fucosylated.

The antimicrobial activity of LF is due to iron sequestration at sites of infection,
depriving the microorganism of this nutrient. Another mechanism is the direct interaction
of the LF molecule with the infectious agent.

Emerg Med Open J. 2023; 9(1): 13-20. doi: 10.17140/EMOJ-9-168