Ultra‐high resolution crystal structure of recombinant caprine β‐lactoglobulin

Crowther, Jennifer M.; Lassé, Moritz; Suzuki, Hisao; Kessans, Sarah A.; Loo, Trevor S.; Norris, Gillian E.; Hodgkinson, Alison J.; Jameson, Geoffrey B.; Dobson, Renwick C. J.

doi:10.1016/j.febslet.2014.09.010

Cited by 15 publications

(10 citation statements)

References 30 publications

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“…1A and 1C to Fig. 1B and 1D), despite the proteins having a very high level of sequence and structural identity (22). As the same concentration of β-lactoglobulin was added to each sample, this suggests that the A isoform of bovine β-lactoglobulin (used in these interaction studies) has a higher binding affinity for the interacting component than caprine β-lactoglobulin.…”

Section: Resultsmentioning

confidence: 99%

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Interactions in milk suggest a physiological role for β-lactoglobulin

Crowther

Broadhurst

Laue

et al. 2019

Preprint

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6β-Lactoglobulin is the most abundant protein in the whey fraction of ruminant milks, yet is 7 absent in human milk. It has been studied intensively due to its impact on the processing and 8 allergenic properties of ruminant milk products. However, the physiological function of β-9 lactoglobulin remains unclear. Sedimentation velocity experiments have identified new 10 interactions between fluorescently-labelled β-lactoglobulin and other components in milk. 11Co-elution experiments support that these β-lactoglobulin interactions occur naturally in milk 12 and provide evidence that the interacting partners are immunoglobulins, while further 13 sedimentation velocity experiments confirm that an interaction occurs between these 14 molecules. Ruminants (e.g. cows and goats) are born without circulating immunoglobulins, 15 which they must obtain from their mothers' milk, whilst humans obtain immunoglobulins 16 both through milk and during gestation via the placenta. We propose that β-lactoglobulin 17 serves to protect immunoglobulins within ruminant milk during digestion, ensuring their 18 efficient transfer from mother to offspring. 19 20 Statement of Significance 21 β-Lactoglobulin is an abundant protein in the whey fraction of ruminant milks (e.g. cow and 22goat milk), yet it is completely absent in human milk. While this protein has been extensively 23 studied, due to its impact on the processing and allergenic properties of milk, its 24 physiological function remains unclear. We fluorescently labelled β-lactoglobulin to monitor 25 its interactions with other milk components within its physiological environment, milk. 26Under these near physiological conditions β-lactoglobulin is capable of interacting with 27 several classes of immunoglobulins. Immunoglobulins are susceptible to digestion, but are 28 required to confer immunity from the mother to the offspring. We propose that β-29 lactoglobulin serves to protect immunoglobulins within ruminant milk during digestion, 30 ensuring their efficient transfer from mother to offspring. 31 32

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Section: Resultsmentioning

confidence: 99%

“…The cloning, expression and purification of recombinant bovine β-lactoglobulin A and caprine β-lactoglobulin have been described in detail previously (21,22).…”

Section: Methodsmentioning

confidence: 99%

Interactions in milk suggest a physiological role for β-lactoglobulin

Crowther

Broadhurst

Laue

et al. 2019

Preprint

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“…Crystal structures of ovine (sheep) [16,17], caprine (goat) [18,19] and reindeer βLg [20] indicate that these orthologues share a high degree of structural similarity with bovine βLg, at both the tertiary and quaternary level (Figure 3), with minimal root-mean-square deviations when aligning the C-α atoms of these structures ( Table 1). However, there are significant differences between the structures of these orthologues and that of porcine βLg, which in the crystal structure features a completely different quaternary association [21].…”

Section: Structure Of βLgmentioning

confidence: 99%

“…The ultrahigh resolution crystal structures of caprine and ovine βLg [17,18] make it possible to clearly define features that in lower resolution bovine and reindeer βLg structures are obscured by disorder and conformational promiscuity. These features include the long flexible CD and GH loops, the C-terminal region, and the AB loops at the dimer interface.…”

Section: Structure Of βLgmentioning

confidence: 99%

Structure, Oligomerisation and Interactions of β-Lactoglobulin

Crowther¹,

Jameson²,

Hodgkinson³

et al. 2016

Milk Proteins - From Structure to Biological Properties and Health Aspects

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β-Lactoglobulin (βLg), as the most abundant whey protein in ruminant milk and as a useful model protein, is the subject of countless biophysical studies in the literature, yet its physiological role is hitherto unknown. This chapter deals with studies that focus on the structure of βLg, its oligomeric behaviour and the interactions that this protein participates in. These and further studies are necessary to understand how the protein's physicochemical properties may influence the processing, digestion and immunogenicity of ruminant milks and their products. However, there is also a need for research into the interactions that occur naturally between βLg and other components in milk, as this may give us insight into the physiological role of the protein.

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“…A brief comparison of the triclinic form (PDB entry 4nlj) will be made here. After the present article had been submitted we also became aware of the deposited coordinates (PDB entry 4tlj; Crowther et al, 2014) of the 1.17 Å resolution structure of recombinant goat -Lg (cf. the sheep A variant) crystallized at pH 6.8 from an alcohol-PEG solution.…”

Section: Introductionmentioning

confidence: 99%

Ovine β-lactoglobulin at atomic resolution

Kontopidis¹,

Gilliver²,

Sawyer³

2014

Acta Cryst Sect F

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The crystal structure of the triclinic form of the milk protein β-lactoglobulin from sheep (Ovis aries) at 1.1 Å resolution is described together with a comparison of the triclinic structures of the low-pH bovine and high-pH ovine proteins. All three structures are remarkably similar, despite the well known pH-dependent conformational transition described for the bovine and porcine proteins that occurs in solution. The high resolution of the present structure determination has allowed a more accurate description of the protein than has hitherto been possible, but it is still not clear whether flexibility changes in the external loops can compensate for the presence of a significant void in the unliganded interior of the structure.

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Ultra‐high resolution crystal structure of recombinant caprine β‐lactoglobulin

Cited by 15 publications

References 30 publications

Interactions in milk suggest a physiological role for β-lactoglobulin

Interactions in milk suggest a physiological role for β-lactoglobulin

Structure, Oligomerisation and Interactions of β-Lactoglobulin

Ovine β-lactoglobulin at atomic resolution

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