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Applied and Environmental Microbiology, July 2001, p. 2883-2894, Vol. 67, No. 7
Antifungal Proteins
Department of Cellular and Structural
Biology, University of Colorado Health Sciences Center, and
MycoLogics, Inc., Denver, Colorado 80262
Fungi are amazing organisms, being
able to use almost any surface (e.g., bathroom tile, skin, or leaves)
for growth. Unfortunately, they also are proficient at colonizing and
using plants, humans, and animals as substrates. During the last two
decades, the incidence of human fungal infections, especially involving
immunocompromised patients, has dramatically increased (27, 41,
57). This is in part due to the tremendous advances in medicine
that permit the saving of patients with neoplastic and
immunocompromising diseases who would otherwise not have survived. It
is ironic that many of these patients succumb to fungal infections for
which there are few or no drugs available for treatment. Encouragingly, naturally occurring antifungal proteins and peptides, as well as
synthetic derivatives, have the potential to be very interesting clinical leads.
Fungi are an extremely diverse group of organisms, with about 250,000 species widely distributed in essentially every ecosystem. Muller and
Loeffler (124) estimate that the weight of fungi on Earth
exceeds that of humans; Armillaria bulbosa, a tree root pathogen, is reported to be among the largest and oldest organisms on
the planet (162). Humans and other animals are exposed to fungi from the moment of birth. Fortunately, only 200 or so species are
pathogenic to mammals, although many nonpathogenic fungi cause allergy
symptoms (3). The majority of fungal exposures and infections are self-limiting in intact animal hosts (76).
However, in patients with compromised immune systems, infections even
by fungal organisms with low virulence can be life threatening; for example, systemic fungal infections of leukemia patients account for
50% of fatalities (101, 141). Nosocomial bloodstream
infections have a similar fatality rate (107).
Plants are also exposed to a large number of pathogenic fungi; although
they do not have an immune system, plants have evolved a variety of
potent defense mechanisms, including the synthesis of
low-molecular-weight compounds, proteins, and peptides that have
antifungal activity (16, 18, 47, 80, 104, 127, 151, 159,
177). Similarly, bacteria, insects, mollusks, fungi, and mammals
synthesize a number of proteins and peptides that are antifungal
(13, 19, 20, 30, 49, 51-54, 58, 68, 69, 79, 83, 109-111, 122,
126, 128, 153, 188, 189, 192). These proteins appear to be
involved in either constitutive or induced resistance to fungal attack.
It is a testament to the efficacy of these defenses that plants and
animals, including humans, do so well against pathogenic fungi.
There are hundreds of antifungal peptides and proteins known, with more
being discovered almost daily. This brief review will focus on proteins
with molecular masses of greater than ~5 kDa, about 50 amino acids in
length; this choice is somewhat arbitrary, for there is not consensus
concerning where a peptide ends and a protein begins. Even eliminating
the small proteins (peptides), the list of antifungal proteins is large
and daunting. The reader is directed to a review concerning antifungal
peptides and proteins of less than 5 kDa (30). Given the
diverse and varied types of proteins, this review will be an overview
of the primary classes of antifungal proteins. Thirteen classes of
antifungal proteins will be described: PR-1 proteins,
(1,3) The fungal cell wall protects the organism against a hostile
environment and relays signals for invasion and infection of a likely
plant, animal, or human host. The cell wall of fungi and yeasts is
synthesized at each hyphal apex in a complex assembly sequence
(45, 105, 149). For example, the walls of Neurospora crassa and Candida albicans are composed of chitin,
(1-3)
0099-2240/01/$04.00+0 DOI: 10.1128/AEM.67.7.2883-2894.2001
Copyright © 2001, American Society for Microbiology. All rights reserved.
MINIREVIEW
INTRODUCTION
Top
Introduction
Conclusion
References
-glucanases, chitinases, chitin-binding proteins,
thaumatin-like (TL) proteins, defensins, cyclophilin-like protein,
glycine/histidine-rich proteins, ribosome-inactivating proteins (RIPs),
lipid-transfer proteins (LTPs), killer proteins (killer toxins),
protease inhibitors, and other proteins. These proteins have been named
primarily on the basis of either their mechanism of action, (e.g.,
glucanases), their structure (e.g., cysteine rich), or their similarity
to a known "type" protein. To confuse the nomenclature further is
the fact that several proteins can be and have been classified into
more than one group. It is unfortunate that a standard nomenclature
based on structure or some other unifying property(ies) of these
proteins has not been proposed or adopted.
FUNGAL CELL WALL STRUCTURE
-D-glucan, (1,6)-glucans, lipids, and peptides
embedded in a protein matrix. The fungal wall affords a clear and
discernible difference between fungi and their plant and animal hosts,
providing an experimental target for antifungal antibiotics. A
schematic of a typical fungal cell wall is shown in Fig.
1. It is important to note that fungi have significant internal turgor pressure so that even slight perturbation of the cell wall results in fungal cell lysis (54, 73, 118-120).
View larger version (47K):
[in a new window]
FIG. 1.
Schematic of fungal cell wall. GPI,
glycophosphatidylinositol.
Several classes of antifungal proteins involve inhibition of the synthesis of the fungal cell wall or disrupt cell wall structure and/or function; others perturb fungal membrane structure, resulting in fungal cell lysis. The assays for antifungal activity include microtiter broth assays, agar diffusion assays, broth microdilution assays (43), and in planta assays (the determination of resistance of transgenic plants overexpressing a protein of interest). Most of the antifungal proteins described below are quite potent, with MICs in the micromolar or microgram-per-milliliter range, equivalent to MICs of many of the currently used agricultural and pharmaceutical antifungal compounds.
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ANTIFUNGAL PROTEINS |
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PR proteins. Plants when exposed to pathogens such as fungi and viruses produce low-molecular-weight antimicrobial compounds called phytoalexins, antimicrobial peptides, and small proteins (e.g., thionins [11, 40], defensins [14], hevein-like proteins, and knottin-like peptides [154]) and up-regulate a number of antimicrobial proteins. These plant proteins, called pathogenesis-related (PR) proteins, have been classically divided into five groups, PR-1, -2, -3, -4, and -5, based on serological and amino acid sequence analyses (180). Recently, another 6 groups of proteins have been suggested for inclusion as PR proteins, bringing the total to 11 groups. The reader is directed to a number of reviews concerning PR proteins, their regulation, and possible roles in plant defense (80, 163, 180, 194).
Each of the five classical groups of PR proteins has two subclasses: a basic subclass found in the plant cell vacuole and an acidic subclass usually found in the extracellular space (reference 80 and references therein). Each group has members with antifungal activity, and cognates of most groups have been found in a diversity of other organisms. The mechanisms of antifungal action of only the PR-2 and PR-3 groups of proteins have been clearly identified.(i) PR-1 proteins.
PR-1 proteins are accumulated to high
levels after pathogen infection and are antifungal both in planta
(transgenic plants overexpressing tobacco PR-1) and in vitro
(129, 165). PR-1 proteins have been found in rice, wheat,
maize, tobacco, Arabidopsis thaliana barley, and many other
plants (1, 15, 117, 125, 145); an alignment of seven PR-1
proteins is shown in Fig. 2. Note that although these proteins are from diverse sources, they are remarkably similar (at least 35% identity). PR-1 proteins have antifungal activity at the micromolar level against a number of plant pathogenic fungi, including Uromyces fabae, Phytophthora infestans, and
Erysiphe graminis (129). PR-1 proteins have
molecular masses of ~15 to 17 kDa and have homology to the
superfamily of cysteine-rich proteins. Although the precise mechanism
of antifungal activity is not understood for plant PR-1 proteins, a
PR-1-like protein, helothermine, from the Mexican banded lizard
interacted with membrane-channel proteins of target cells, inhibiting
the release of Ca2+ (123). Whether antifungal
plant PR-1 proteins act by this mechanism is not known but is
suspected.
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(ii) PR-2 proteins (-glucanses).
PR-2 proteins have
(1,3)-endoglucanase activity in vitro and have been grouped into
three classes on the basis of amino acid sequence analysis (8,
25, 95, 103, 113, 131, 140). Class I glucanases are basic
proteins of ~ 33 kDa and are found in the plant vacuole. Classes
II and III include acidic, extracellular proteins of about 36 kDa. The
major structural difference between class I proteins and the other two
classes is that class I proteins are synthesized as preproproteins that
are processed prior to being enzymatically active. PR-2 proteins have
been found in a wide variety of plants, including tobacco, A. thaliana, peas, grains, and fruits (25, 77, 146); the
proteins are active in vitro at micromolar levels (~50 µg/ml)
against a wide number of fungi, including human and plant pathogens
(e.g., Rhizoctonia solani, C. albicans, and
Aspergillus fumigatus). The antifungal activity of PR-2
proteins has been convincingly demonstrated by a number of in vitro
enzyme and whole-cell assays (163) as well as in planta
using transgenic plants overexpressing a PR-2 protein (71).
-glucanases is thought to
occur by PR-2 proteins hydrolyzing the structural (1,3)-glucan present in the fungal cell wall, particularly at the hyphal apex of
filamentous molds where glucan is most exposed, resulting in a cell
wall that is weak. This weakened cell wall results in cell lysis and
cell death.
(iii) PR-3 proteins (chitinases). A number of enzymatic assays have shown PR-3 proteins to have in vitro chitinase activity. Most PR-3 proteins have molecular masses of between 26 and 43 kDa (131, 187). Chitinases (both plant PR-3 chitinases and chitinases from other sources) have been divided into five groups. class I chitinases contain an N-terminal cysteine-rich domain of ~40 amino acids (also known as the wheat germ agglutinin domain), a chitin-binding hevein-like domain, a highly conserved central portion, and a hinge region; most class I proteins have molecular masses of ~32 kDa. Class II proteins are similar in amino acid sequence to class I proteins, but they lack the N-terminal cysteine-rich domain and have molecular masses of 27 to 28 kDa. Class IV proteins resemble class I chitinases but are significantly smaller due to four major deletions. Class III proteins do not share amino acid sequence homology to any other class and have molecular masses of ~28 to 30 kDa. Class V chitinases show sequence similarities to bacterial exochitinases and have molecular masses of 41 to 43 kDa. In addition to chitinases, a chitosanase (chitosan is deacetylated chitin) from Streptomyces strain N174 with antifungal activity has been isolated (119), and its X-ray structure has been determined.
Chitinases have been isolated from fungi (74, 112), plants (tobacco [114], cucumber, beans [198], peas, grains [63], and many others [37, 96, 112, 121, 150, 193]), and bacteria (22) and have potent antifungal activity against a wide variety of human and plant pathogens, including Trichoderma reesei, Alternaria solani, A. radicina, Fusarium oxysporum, R. solani, Guignardia bidwellii, Botrytis cinerea, and Coprinus comatus. By analogy with-glucanases, the mode of action of PR-3 proteins is relatively straightforward: PR-3 proteins are endochitinases that cleave cell wall
chitin polymers in situ, resulting in a weakened cell wall and
rendering fungal cells osmotically sensitive. Not surprisingly, PR-2
(-glucanases) and PR-3 (chitinases) proteins act synergistically in
inhibiting fungal growth, both in vitro and in planta
(71).
(iv) PR-4 (chitin-binding) proteins.
PR-4 proteins are
chitin-binding proteins, have molecular masses of 13-14.5 kDa, and have
been classified into two groups (42, 56, 143, 179). Class
I proteins have amino acid sequence similarities to hevein (a
chitin-binding polypeptide [42, 85, 179]) and belong to
the superfamily of chitin-binding lectins. Class II proteins lack the
chitin-binding domain. PR-4 proteins have been isolated from potato,
tobacco, barley, tomato, and many other plants (42, 56, 85, 143,
179); an alignment of six PR-4 proteins is shown in Fig.
3. Note that the PR-4 proteins from the
diverse sources share common sequences. Both classes of proteins have
potent antifungal activity against a wide variety of human and plant
pathogens (e.g., Trichoderma harzianum, Fusarium culmorum, F. graminearum, and B. cinerea). The antifungal activity of class I proteins is likely the result of protein binding to nascent
fungal cell wall -chitin. By mechanisms not understood, this results
in disrupted cell polarity, with concomitant inhibition of growth
(13). The mechanism of action of class II proteins (which
lack the chitin-binding hevein domain but are antifungal nonetheless)
is not understood.
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(v) PR-5 (TL) proteins. PR-5 proteins share significant amino acid homology to thaumatin (a sweet-tasting [to humans] protein from the South African ketemfe berry bush) and are known as TL proteins. TL proteins have been isolated from A. thaliana (59, 60), corn (62, 148), soybeans, rice, wheat, tobacco (81), tomato (161), pumpkin (21), beans (196), barley (55), flax (12), and many other plants (122, 182, 184). The majority of PR-5 proteins have molecular masses of ~22 kDa and are stabilized by eight disulfide bonds. This highly stabilized structure allows PR-5 proteins to be very resistant to protease degradation (148). The X-ray structures have been determined for two PR-5 proteins and thaumatin (82, 134).
Although the precise mechanism of action of PR-5 proteins is not completely understood, there are a number of interesting observations that may eventually lead to a unified hypothesis for how these proteins function to kill fungi (24, 66, 147, 158, 186). First, several TL proteins cause cell permeability changes in fungal cells with a cell wall but have no or little effect on protoplasts (148). For example, zeamatin (a TL protein from corn) caused very rapid cell lysis of N. crassa, even at 4°C; lysis occurred primarily at subapical regions (148). Second, a number of PR-5 proteins bind (1,3)-glucan and have
detectable in vitro (1,3)-glucanase activity (47, 176).
Third, zeamatin inhibits insect 
-amylase and mammalian trypsin
activities in vitro (152a). Fourth, osmotin, a TL protein
from tobacco, causes perturbations in the regulation of fungal cell
wall assembly (200, 201). Fifth, zeamatin and nikkomycin
act in synergy, reducing the amount of zeamatin required for cell
killing up to 1,000-fold (148). These disparate
observations are difficult to assimilate into one mechanism of action.
Regardless of the precise mode of action of TL proteins, they are
fungicidal against a wide number of plant and human pathogens in vitro.
Importantly, one protein, zeamatin, has shown efficacy in a
murine vaginal model of C. albicans infection (D. A. Stevens et al., submitted for publication). It may be that certain
PR-5 proteins can be developed into human therapeutics.
Defensins. Defensins are a diverse group of low-molecular-mass cysteine-rich proteins found in mammals, fungi (89), insects (91), and plants (14, 16). The insect and mammalian defensins are quite small (3 to 5 kDa) and form voltage-dependent ion channels in plasma membranes (92, 93, 171). Thionins are also small (3 to 5 kDa) cysteine-rich peptides that are toxic to fungi (171). Neither the mammalian defensins, insect defensins, nor thionins will be described in this review, for they are generally smaller than 5 kDa.
Plant and fungal defensins are cysteine-rich proteins ranging from 45 to 54 amino acids, are positively charged, and in most cases contain four disulfide bonds that stabilize each protein in solution (4, 5, 38, 49, 87, 88, 106, 110, 135, 155, 168, 169, 170, 181). In addition, most defensins are highly oligomeric (many subunits of 4 to 5 kDa) in situ (168, 169). Defensins are classified into four groups. Group I defensins cause morphological changes in susceptible fungi and are known as morphogenic defensins, group II proteins inhibit fungal growth but do not cause morphological changes (nonmorphogenic group), group III are inactive against test fungi but inhibit-amylases in vitro, and group IV are unique in terms of
antifungal specificity and structure (155). An amino acid
alignment of a number of plant and fungal defensins is shown in Fig.
4. Note the high degree of similarity
within each group. In addition, the positions of the cysteine residues
are conserved in group I, II, and III proteins. No other significant
homology exists between groups.
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Cyclophilin-like protein.
Cyclophilins are a highly conserved
group of proteins that are the intracellular receptors for cyclosporin;
they have been found in a wide variety of organisms, including
bacteria, plants, animals, and fungi (137). Recently an
18-kDa protein was isolated from mung bean (Phaseolus mungo)
with activity against R. solani, F. oxysporum, B. cinerea,
and Coprinus comatus (199). This protein, called mungin, showed significant homology to cyclophilins and inhibited - and -glucosidases in vitro. However, the antifungal mechanism of action of mungin is not known.
Glycine/histidine-rich proteins.
Insects synthesize a number
of glycine/histidine-rich antifungal proteins and polypeptides,
including those from Holotrichia diomphalia larvae
(holotrichin, 84 amino acids [97]), Sarcophaga peregrina (flesh fly, AFP, 67 amino acids [68]),
and Tenebrio molitor (tenecin, 49 amino acids [28,
96, 98, 99]). An alignment of these proteins is shown in Fig.
5. Note that they are extremely rich in
glycine and histidine, which comprise as much as 80% of the amino
acids. Importantly, fungi inhibited included C. albicans,
the most common human pathogen (e.g., the 50% inhibitory concentration
of tenecin is ~8 µg/ml [28]). The mechanism of action of these proteins is not understood.
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RIPs.
RIPs are RNA N-glycosidases that depurinate
rRNA, resulting in the arrest of protein synthesis due to ribosome
damage (7, 39, 65, 94, 144, 167). Plant RIPs inhibit
mammalian, bacterial, fungal, and plant protein syntheses in vitro and
in vivo (67). As an aside, how plants protect themselves
from the action of their own RIPs is a subject of very interesting
research. RIPs have been classified into three groups. Type 1 RIPs are
single-chain N-glycosidases with molecular masses of 11 to
30 kDa. Type 2 RIPs contain two chains, a cell-binding lectin (B chain)
and an N-glycosidase (A chain), with molecular masses of
~60 kDa (202); type 2 RIPs include toxic members such as
ricin and nontoxic members such as ebulin 1 (44) and
nigrin b. Type 3 RIPs consist of four chains organized as two dimers of
type 2 RIPs. RIPs have been isolated from a number of plants
(Mirabilis expansa [183], Pisum
sativum [90, 197] Momordica charantia
[100], Ricinus communis [6], Viscum album, and many others [35, 50, 102, 138, 178,
185, 190, 195]) as well as from fungi, e.g., Aspergillus
giganteus (-sarcin [51, 188]) Unfortunately, the
antifungal activities of only a few of the many RIPs have been described.
LTPs.
LTPs have the ability to transfer phospholipids between
membranes. LTPs are small proteins (~8.7 kDa) of ~90 amino acids
stabilized by four disulfide bonds with a central tunnel-like
hydrophobic cavity. They have been isolated from a number of sources,
including mammals, plants, fungi, and bacteria (17, 26, 115, 116, 130, 154, 166, 175), and may play several in vivo roles,
including lipid exchange between cytoplasmic organelles and,
importantly, defense against pathogens (48). An alignment
of a number of LTPs is shown in Fig. 6.
Note that although the proteins are from diverse sources, they have
striking homologies (between 37 to 90% identity). LTPs are active in
vitro against a number of bacteria and fungi; however, the mechanism of
action is not known. It may be that these proteins insert themselves
into the fungal cell membrane, and the central hydrophobic cavity forms
a pore, allowing efflux of intracellular ions and thus leading to
fungal cell death. How this is related to their lipid transfer function
is not clear.
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Killer proteins (killer toxins).
A number of yeasts secrete
proteins that are lethal to sensitive fungal cells. These proteins,
called killer proteins or killer toxins, are encoded either by
double-stranded RNA, linear double-stranded plasmid DNA, or nuclear
genes (2, 23, 70, 108, 153). Fungal cells secreting a
killer toxin are resistant to their own toxin but are sensitive
to other toxins. Saccharomyces cerevisiae, Ustilago maydis,
Hanseniaspora uvarum, Zygosaccharomyces bailii, Phaffia rhodozyma,
Kluveromyces lactis, and several Pichia species secrete
a number of killer proteins (reviewed in reference 108). Over 20 individual killer toxins have been identified, varying in
molecular mass from 10.7 to 156.5 kDa (58, 84). The killer toxins have broad, potent antifungal activity against a number of human
and plant pathogens (including Pneumocystis carinii
[157])
MICs vary from 20 µg/ml to far less. Although
they have varied mechanisms of action, the first step of killer protein
activity involves binding of the protein to specific cell surface
receptors. Once bound, killer proteins are internalized and can disrupt
cell wall synthesis, DNA synthesis, and K+ channel
activity, inhibit (1,3)-glucan synthesis, or arrest the cell cycle
(2, 36, 78, 79, 164). Any one of these effects leads to
inhibition of fungal growth and to fungal cell death.
Protease inhibitors. Protein inhibitors of serine (e.g., trypsin and chymotrypsin) and cysteine proteases have emerged as a class of antifungal proteins that have potent activity against plant and animal pathogens. Cysteine protease inhibitors have been isolated from a number of plants and form a fourth group of cystatins, the phytocystatins (10, 72, 86, 139). The phytocystatins are single polypeptides of 10 to 12 kDa and share common structural motifs. Although phytocystatins are active against plant pathogens such as F. solani (MIC of 20 µg/disk in an disk agar diffusion assay) and Trichoderma reesei (250 ng/disk) (72), the mechanism of antifungal activity is not understood.
Serine protease inhibitors that have antifungal activity also have the interesting property of inhibiting-amylase activity from insects
but not from bacterial or mammalian sources (152a). These
proteins are bifunctional, inhibiting enzymes as well as inhibiting
insect and fungal growth. Blanco-Labra and Iturbe-Chinas identified a
bifunctional -amlyase/trypsin inhibitor from corn (10);
later it was found that this protein was identical to zeamatin
(147, 148). We have recently confirmed that at high trypsin/zeamatin and -amylase/zeamatin molar ratios, zeamatin inhibits trypsin and insect -amylase activities in vitro
(152a). Other bifunctional proteins from ragi
(Eleusine coracana), wheat, and barley have been isolated
and characterized (9, 46, 133, 152, 160). Only a few of
these proteins have been tested for in vitro antifungal activity, with
zeamatin being the most extensively characterized. The mechanism of
antifungal activity of these proteins is not fully understood.
Other proteins. New proteins that have antifungal activity but do not neatly fall into any of the above classes are being discovered at a rapid pace. Only a few can be mentioned here. Viridin, a novel protein isolated from the culture medium of Trichoderma viride, has a molecular mass of 65 kDa and is active against sensitive fungi at 6 µM (52, 53). Snakin-1 isolated from potato has a molecular mass of 6.9 kDa and is active at 10 µM (156). A 30-kDa protein with very potent antifungal activity (50 ng/disk in an agar diffusion assay) was isolated from Engelmann's daisy (Engelmannia pinnatifida); this protein showed 35 to 50% identity to self-incompatibility glycoproteins, not previously known to be antifungal (64). The mechanism of action of none of these proteins is known.
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CONCLUSIONS |
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Top
Introduction
Conclusion
References
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Antifungal proteins and polypeptides have been isolated from diverse groups of organisms, including plants, fungi, bacteria, insects, and animals (both vertebrates and invertebrates). The mechanisms of action of these proteins are as varied as their sources and include fungal cell wall polymer degradation, membrane channel and pore formation, damage to cellular ribosomes, inhibition of DNA synthesis, and inhibition of the cell cycle. The mode of action of many proteins remains unknown and is the subject of active research. The range of fungi inhibited by antifungal proteins is extremely broad, with plant pathogens and humans pathogens being sensitive at micromolar levels; in some cases, even more potent inhibition was found.
The genes encoding many antifungal proteins are currently being used by agribusiness to create genetically modified plants that have increased fungal resistance in the field. Whether these transgenic plants and the crops derived from them gain acceptance in the marketplace remains to be seen. Equally important, antifungal proteins and peptides are being tested for use as pharmaceutical agents for the treatment of human and animal fungal diseases. This is particularly exciting since the modes of action of these proteins are vastly different from the currently used therapeutics, resistance to which is becoming a clinical problem. There are a number of antifungal proteins in various stages of preclinical development, and the results of these experiments and of the subsequent human clinical trials are eagerly anticipated.
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ACKNOWLEDGMENTS |
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This review could not have been completed without the much needed assistance of Samatha Renault, Rebecca Schimoler-O'Rourke, Shelly Wilson, and Tamara Kay Miller.
This work was supported by institutional funds from MycoLogics, Inc.
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FOOTNOTES |
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* Mailing address: University of Colorado Health Sciences Center, Department of Cellular and Structural Biology, Denver, CO 80262. Phone: (303) 315-8647. Fax: (303) 315-4024. E-mail: Claude.Selitrennikoff{at}uchsc.edu.
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REFERENCES |
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Introduction
Conclusion
References
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Applied and Environmental Microbiology, July 2001, p. 2883-2894, Vol. 67, No. 7
0099-2240/01/$04.00+0 DOI: 10.1128/AEM.67.7.2883-2894.2001
Copyright © 2001, American Society for Microbiology. All rights reserved.
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