Immunoglobulin-binding domains: Protein L from Peptostreptococcus magnus

Housden, Nicholas G.; Harrison, S.; Roberts, S.E.; Beckingham, Jennifer A.; Graille, Marc; Stura, E.A.; Gore, Michael G.

doi:10.1042/bst0310716

Cited by 35 publications

(26 citation statements)

References 27 publications

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“…MID (200 kDa), also referred to as Hag, has been found to be responsible for M. catarrhalis binding to soluble IgD and for the stimulation of high-density IgD-bearing B lymphocytes (42)(43)(44)109). In fact, nonimmune binding of Igs by gram-positive bacteria is relatively common but rare among gram-negative bacteria (51,75). Interestingly, H. influenzae also displays a strong affinity for soluble human IgD (125), although the protein involved in IgD binding has as yet been identified only in M. catarrhalis.…”

Section: Adhesion and Major Ompsmentioning

confidence: 99%

Molecular Aspects ofMoraxella catarrhalisPathogenesis

Vries

Bootsma

Hays

et al. 2009

Microbiol Mol Biol Rev

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SUMMARY In recent years, Moraxella catarrhalis has established its position as an important human mucosal pathogen, no longer being regarded as just a commensal bacterium. Further, current research in the field has led to a better understanding of the molecular mechanisms involved in M. catarrhalis pathogenesis, including mechanisms associated with cellular adherence, target cell invasion, modulation of the host's immune response, and metabolism. Additionally, in order to be successful in the host, M. catarrhalis has to be able to interact and compete with the commensal flora and overcome stressful environmental conditions, such as nutrient limitation. In this review, we provide a timely overview of the current understanding of the molecular mechanisms associated with M. catarrhalis virulence and pathogenesis.

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Section: Adhesion and Major Ompsmentioning

confidence: 99%

Molecular Aspects ofMoraxella catarrhalisPathogenesis

Vries

Bootsma

Hays

et al. 2009

Microbiol Mol Biol Rev

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“…This loop is involved in Fc binding in SpG (51,52). Its absence in PpL is thought to be related to the inability of PpL to bind to bind Fc (53).…”

Section: Purification and Biophysical Characterization Of Recombinantmentioning

confidence: 99%

Crystal Structure of a Mucus-binding Protein Repeat Reveals an Unexpected Functional Immunoglobulin Binding Activity

MacKenzie

Tailford

Hemmings

et al. 2009

Journal of Biological Chemistry

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Lactobacillus reuteri mucus-binding protein (MUB) is a cellsurface protein that is involved in bacterial interaction with mucus and colonization of the digestive tract. The 353-kDa mature protein is representative of a broadly important class of adhesins that have remained relatively poorly characterized due to their large size and highly modular nature. MUB contains two different types of repeats (Mub1 and Mub2) present in six and eight copies, respectively, and shown to be responsible for the adherence to intestinal mucus. Here we report the 1.8-Å resolution crystal structure of a type 2 Mub repeat (184 amino acids) comprising two structurally related domains resembling the functional repeat found in a family of immunoglobulin (Ig)-binding proteins. The N-terminal domain bears striking structural similarity to the repeat unit of Protein L (PpL) from Peptostreptococcus magnus, suggesting binding in a non-immune Fab-dependent manner. A distorted PpL-like fold is also seen in the C-terminal domain. As with PpL, Mub repeats were able to interact in vitro with a large repertoire of mammalian Igs, including secretory IgA. This hitherto undetected activity is consistent with the current model that antibody responses against commensal flora are of broad specificity and low affinity. The human gastrointestinal tract (GIT)3 contains trillions of bacteria, representing hundreds of species and thousands of subspecies (1). They outnumber our own cells by a factor of 10 and contribute many physiological capabilities, including the provision of metabolic attributes not encoded in the human genome (2). A protective layer of mucus, consisting of a complex mixture of large, highly glycosylated proteins (mucins) (3), covers the epithelial cells of the intestine and offers an attachment site for the colonizing bacteria. These bacteria play important roles in maintaining normal gut function and in building resistance of the host to pathogenic micro-organisms (4, 5). Some may use mucins as their major carbon and energy source (6, 7).Lactobacilli are Gram-positive microaerophilic bacteria naturally present in the dominant colonic microbiota and have been considered to be beneficial for human health (8). They are commonly used as probiotics, which are defined by the Food and Agriculture Organization/World Health Organization as live microorganisms that, when administered in adequate amounts, confer a health benefit on the host (9). As probiotic agents, lactobacilli can prevent or alleviate infectious diarrhea through their effects on the immune system and promote host resistance to colonization by pathogens (10, 11), and many have been shown to adhere to intestinal mucus (12-19). Confirmation of this lactobacillus-mucus association has not only been observed in vitro, but has also been validated by ex vivo/in vivo microscopic analysis of biopsy samples (20,21). In most cases, lactobacilli adhesion to mucus has been proposed to be mediated by proteins (22-30). Compared with the present understanding of the adhesive mechanisms of human...

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“…As the binding site for Protein L resides in framework region 1 of the variable domain of kappa light chain subtypes (kappa I, III, and IV from humans and kappa I and V from mice) [94,96,110], fragments derived from antibodies that have kappa light chain subtypes can be purified using Protein L [100]. Since Protein L interacts with the light chain, it has no immunoglobulin class restrictions and offers the potential of being a "broadly if not generally" useful affinity ligand [109]. Approximately 60% of mammalian IgG light chains are kappa chains, with the remaining 40% being lambda chains that lack binding sites for Protein L [73,98].…”

Section: Protein L and Its Use In Antibody Fragment Bioprocessingmentioning

confidence: 99%

“…Such affinity resins have been used in the noncommercial purification of scFv's [31,41,80,89,105,106], Fab's [91,[106][107][108], and single-domain antibodies [52,91,98,103,108,109].…”

Section: Protein L and Its Use In Antibody Fragment Bioprocessingmentioning

confidence: 99%

Antibody Fragments and Their Purification by Protein L Affinity Chromatography

Rodrigo¹,

Gruvegard²,

Alstine

2015

Antibodies

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Antibodies and related proteins comprise one of the largest and fastest-growing classes of protein pharmaceuticals. A majority of such molecules are monoclonal antibodies; however, many new entities are antibody fragments. Due to their structural, physiological, and pharmacological properties, antibody fragments offer new biopharmaceutical opportunities. In the case of recombinant full-length antibodies with suitable Fc regions, two or three column purification processes centered around Protein A affinity chromatography have proven to be fast, efficient, robust, cost-effective, and scalable. Most antibody fragments lack Fc and suitable affinity for Protein A. Adapting proven antibody purification processes to antibody fragments demands different affinity chromatography. Such technology must offer the unit operation advantages noted above, and be suitable for most of the many different types of antibody fragments. Protein L affinity chromatography appears to fulfill these criteria-suggesting its consideration as a key unit operation in antibody fragment processing.

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Immunoglobulin-binding domains: Protein L from Peptostreptococcus magnus

Cited by 35 publications

References 27 publications

Molecular Aspects ofMoraxella catarrhalisPathogenesis

Molecular Aspects ofMoraxella catarrhalisPathogenesis

Crystal Structure of a Mucus-binding Protein Repeat Reveals an Unexpected Functional Immunoglobulin Binding Activity

Antibody Fragments and Their Purification by Protein L Affinity Chromatography

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