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Review
. 2024 May 19;12(5):1026.
doi: 10.3390/microorganisms12051026.

A Review of the Mechanisms of Bacterial Colonization of the Mammal Gut

Qingjie Lin  1 , Shiying Lin  1 , Zitao Fan  1 , Jing Liu  2 , Dingcheng Ye  2 , Pingting Guo  1
Affiliations
Review

A Review of the Mechanisms of Bacterial Colonization of the Mammal Gut

Qingjie Lin et al. Microorganisms. .

Abstract

A healthy animal intestine hosts a diverse population of bacteria in a symbiotic relationship. These bacteria utilize nutrients in the host's intestinal environment for growth and reproduction. In return, they assist the host in digesting and metabolizing nutrients, fortifying the intestinal barrier, defending against potential pathogens, and maintaining gut health. Bacterial colonization is a crucial aspect of this interaction between bacteria and the intestine and involves the attachment of bacteria to intestinal mucus or epithelial cells through nonspecific or specific interactions. This process primarily relies on adhesins. The binding of bacterial adhesins to host receptors is a prerequisite for the long-term colonization of bacteria and serves as the foundation for the pathogenicity of pathogenic bacteria. Intervening in the adhesion and colonization of bacteria in animal intestines may offer an effective approach to treating gastrointestinal diseases and preventing pathogenic infections. Therefore, this paper reviews the situation and mechanisms of bacterial colonization, the colonization characteristics of various bacteria, and the factors influencing bacterial colonization. The aim of this study was to serve as a reference for further research on bacteria-gut interactions and improving animal gut health.

Keywords: adhesion; bacterial colonization; colonization resistance; intestine; pathogens; probiotics; receptor.

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Conflict of interest statement

The authors declare no competing interests.

Figures

Figure 1
Figure 1
Fimbrial adhesions. Like type 1 pili in Escherichia coli, fimbriae are mainly composed of various Fim protein subunits, including FimH, FimG, FimF, FimC, and thousands of FimA. The FimH subunit, located at the top, utilizes binding sites (lectins) to bind with α-D-mannose-specific receptors [25].
Figure 2
Figure 2
Afimbrial adhesions. The extracellular carboxy terminus of the enteropathogenic Escherichia coli (EPEC) protein, which is involved in afimbrial adhesion, contains three immunoglobulin domains (D1, D2, and D3) and a terminal C-type lectin cell-binding domain (D4). Intimin binds to the extracellular intimin-binding domain of Tir, Tir-M, to produce the characteristic intimate EPEC adhesion, actin accretion, and attaching/effacing lesion formation (a) [11]. Lactobacillus longum adheres to intestinal epithelial cells through the afimbrial adhesin FimM, which binds to mucin and fibronectin adhesion receptors on the cell surface (b) [26]. In Helicobacter pylori, BabA binds to mucins decorated with Leb blood group antigens. SabA binds to both Lex-sialylated and asialylated Laminin. HpaA can bind to sialic acid, and Hsp60 can bind to sulfatides (c) [27]. The bacterial–host adhesion models mentioned above were derived from the respective cited references and have been modified accordingly.
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