The cryptome: a subset of the proteome, comprising cryptic peptides with distinct bioactivities

Autelitano, Dominic J.; Rajic, Antonio; Smith, A. Ian; Berndt, Michael C.; Ilag, Leodevico L.; Vadas, Mathew A.

doi:10.1016/j.drudis.2006.02.003

Cited by 88 publications

(63 citation statements)

References 80 publications

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“…Peptide release from larger ‘maternal’ proteins is more widespread than once thought. Indeed, the ‘cryptome’ refers to the entire subset of proteins/peptides released from maternal sources, which have alternative or heightened activities [107–109]. Human lactoferrin [110, 111], lysozyme [112] and cathepsin G [113] are more examples of macromolecules containing encrypted peptides.…”

Section: The Oxygen-transport Proteinsmentioning

confidence: 99%

Immunological properties of oxygen-transport proteins: hemoglobin, hemocyanin and hemerythrin

Coates

Decker

2016

Cell. Mol. Life Sci.

123

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It is now well documented that peptides with enhanced or alternative functionality (termed cryptides) can be liberated from larger, and sometimes inactive, proteins. A primary example of this phenomenon is the oxygen-transport protein hemoglobin. Aside from respiration, hemoglobin and hemoglobin-derived peptides have been associated with immune modulation, hematopoiesis, signal transduction and microbicidal activities in metazoans. Likewise, the functional equivalents to hemoglobin in invertebrates, namely hemocyanin and hemerythrin, act as potent immune effectors under certain physiological conditions. The purpose of this review is to evaluate the true extent of oxygen-transport protein dynamics in innate immunity, and to impress upon the reader the multi-functionality of these ancient proteins on the basis of their structures. In this context, erythrocyte–pathogen antibiosis and the immune competences of various erythroid cells are compared across diverse taxa.Electronic supplementary materialThe online version of this article (doi:10.1007/s00018-016-2326-7) contains supplementary material, which is available to authorized users.

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Section: The Oxygen-transport Proteinsmentioning

confidence: 99%

Immunological properties of oxygen-transport proteins: hemoglobin, hemocyanin and hemerythrin

Coates

Decker

2016

Cell. Mol. Life Sci.

123

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“…Typically, the peptides that have been identified arise from the processing of a longer protein precursor. This has led to the suggestion that a 'cryptome' might exist, composed of biologically active peptides with their own separate functions resulting from the processing of well-characterized proteins [7]. A more recent development is represented by studies into uORFs, short ORFs found upstream of long ORFs in canonical transcripts.…”

Section: Introductionmentioning

confidence: 99%

Hundreds of putatively functional small open reading frames in Drosophila

et al. 2011

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BackgroundThe relationship between DNA sequence and encoded information is still an unsolved puzzle. The number of protein-coding genes in higher eukaryotes identified by genome projects is lower than was expected, while a considerable amount of putatively non-coding transcription has been detected. Functional small open reading frames (smORFs) are known to exist in several organisms. However, coding sequence detection methods are biased against detecting such very short open reading frames. Thus, a substantial number of non-canonical coding regions encoding short peptides might await characterization.ResultsUsing bio-informatics methods, we have searched for smORFs of less than 100 amino acids in the putatively non-coding euchromatic DNA of Drosophila melanogaster, and initially identified nearly 600,000 of them. We have studied the pattern of conservation of these smORFs as coding entities between D. melanogaster and Drosophila pseudoobscura, their presence in syntenic and in transcribed regions of the genome, and their ratio of conservative versus non-conservative nucleotide changes. For negative controls, we compared the results with those obtained using random short sequences, while a positive control was provided by smORFs validated by proteomics data.ConclusionsThe combination of these analyses led us to postulate the existence of at least 401 functional smORFs in Drosophila, with the possibility that as many as 4,561 such functional smORFs may exist.

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“…Biologically active peptides, defined as cryptides or crypteins, may also derive from proteolytic cleavage of physiological proteins, including, among others, hemoglobin, components of the complement cascade, and milk proteins [18, 19]. Cryptides may exhibit a broad spectrum of biological activities, different from those of the precursor proteins.…”

Section: Introductionmentioning

confidence: 99%

Antiviral Activity of Synthetic Peptides Derived from Physiological Proteins

et al. 2018

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Background/Aims: New antivirals are needed to supplement or replace currently used drugs. The aim of this study was to evaluate the antiviral activity of synthetic peptides derived from physiological proteins. Methods: Vero cell monolayers were infected with herpes simplex virus 1, vesicular stomatitis virus, adenovirus, and coxsackievirus B5 strains in the presence of different concentrations of the selected peptides and viral yield was determined by plaque reduction assays to evaluate the antiviral activity of the peptides. Virucidal activity was evaluated by determining the residual infectivity of viral suspensions treated for 1 h with the peptides at the same concentrations as in the viral yield assays. Results: Among the investigated peptides, the killer peptide proved to exert a considerable antiviral activity against herpes simplex virus, attributable to a direct effect on virus particles, while its derivative K10S showed to be effective against the four investigated virus strains only at the highest concentration tested, yet, the inhibitory effects were only partial. Conclusion: Overall, initial evidence is provided on the antiviral activity of several peptides, as well as of their derivatives. Further investigation is warranted to ascertain the mechanism of action in order to develop new potential antiviral drugs.

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The cryptome: a subset of the proteome, comprising cryptic peptides with distinct bioactivities

Cited by 88 publications

References 80 publications

Immunological properties of oxygen-transport proteins: hemoglobin, hemocyanin and hemerythrin

Immunological properties of oxygen-transport proteins: hemoglobin, hemocyanin and hemerythrin

Hundreds of putatively functional small open reading frames in Drosophila

Antiviral Activity of Synthetic Peptides Derived from Physiological Proteins

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