Guide · 7 min
Why Your Mouth Tingles After Eating Fruit in Pollen Season
The surprising link between hayfever and the foods that suddenly don't agree with you
In short
Birch pollen allergens, particularly Bet v 1 (a PR-10 pathogenesis-related protein), cross-react with homologous proteins in a wide range of foods including Rosaceae fruits (apple, pear, peach, cherry), Apiaceae vegetables (carrot, celery), nuts (hazelnut, almond), and legumes (soy, peanut)…
Why Your Mouth Itches When You Eat an Apple in Spring
You've eaten apples your whole life without a second thought. Then one spring, somewhere around the time the trees start flowering, you bite into one and your lips tingle, your mouth itches, and your throat feels faintly strange for a few minutes. Nothing dramatic — it passes quickly — but it's unsettling enough that you wonder whether you've suddenly developed a food allergy.
You probably haven't. What you've most likely encountered is pollen-food allergy syndrome (PFAS), sometimes called oral allergy syndrome (OAS) — a phenomenon that affects a significant proportion of hayfever sufferers and is almost entirely driven by your immune system's relationship with the pollen you've been breathing in. Understanding what's actually happening is both reassuring and genuinely useful for managing your season.
The Science: Your Immune System Is Making a Case of Mistaken Identity
When you're sensitised to pollen, your immune system produces IgE antibodies targeted at specific pollen proteins. The problem is that some of those same proteins — or very close structural relatives of them — also exist in plant foods. Your immune system, trained to flag up one thing, ends up reacting to another.
This isn't a coincidence. It's the result of deep evolutionary conservation in plant biology: certain protein families are so structurally similar across grasses, trees, fruits, and vegetables that your immune system genuinely cannot tell the difference.
The birch pollen story is the most thoroughly characterised. Birch's dominant allergen, Bet v 1, belongs to a family of proteins called PR-10 (pathogenesis-related proteins). Homologous versions appear in apple (Mal d 1), hazelnut (Cor a 1), soy (Gly m 4), peanut (Ara h 8), carrot, celery, and Rosaceae fruits including peach, pear, and cherry. Because the amino acid sequence identity between Bet v 1 and these food proteins exceeds 40–60%, IgE antibodies raised against birch pollen readily bind to them (Bohle, 2007). Crucially, Fritsch et al. (1998) demonstrated that this cross-reactivity operates not just at the antibody level but at the T-cell level too — meaning the immune response is reinforced by cellular memory, not just circulating IgE. An estimated 70% of birch-sensitised individuals experience some degree of food cross-reactivity, making this among the most prevalent food-allergy phenomena in temperate regions.
Grass pollen tells a slightly different story, dominated by a different protein family: profilins. Phl p 12 — a profilin from timothy grass — shares greater than 70% sequence identity with profilins found in melons (cantaloupe, watermelon, honeydew), tomatoes, potatoes, oranges, peaches, celery, peanuts, and kiwi (Haidar et al., 2024; Vieths, 1997). Profilins are actin-binding proteins ubiquitous across the plant kingdom, which is precisely why grass pollen sensitisation casts such a wide dietary net. Grass pollen also carries a secondary cross-reactive allergen, Phl p 14, which belongs to the non-specific lipid transfer protein (nsLTP) family. Unlike PR-10 proteins and profilins, nsLTPs are thermostable and resistant to digestion — a distinction that matters clinically, as we'll see.
The result of all this molecular mimicry? Eating certain raw foods triggers localised mast cell degranulation in your oral mucosa — the lining of your lips, mouth, and throat. Symptoms typically appear within minutes: tingling, itching, mild swelling of the lips or tongue, a scratchy throat. They usually resolve within 30 minutes without intervention. The reason reactions stay local is that most of these cross-reactive proteins (particularly PR-10 proteins and profilins) are heat-labile and structurally fragile — they're rapidly broken down by stomach acid and digestive enzymes before they can be absorbed systemically (Vieths et al., 2002).
What This Means for You
If you have birch pollen hayfever, the foods most likely to give you oral symptoms are raw apple, pear, peach, cherry, hazelnut, carrot, and celery. If grass pollen is your main trigger, your list extends to melons, tomatoes, kiwi, and oranges — alongside some overlap with the birch list.
A few things are worth knowing:
Cooking usually solves the problem. Because the relevant proteins are heat-labile, cooking, microwaving, or even thoroughly stewing most of these foods destroys the cross-reactive structure. Stewed apple, cooked carrot, tinned peaches — these are typically well tolerated, even by people who react to the raw versions. Processing works similarly: pasteurised apple juice is generally fine where fresh-pressed juice isn't. This is supported by evidence from both in vitro IgE-binding studies and clinical observations (Effect of Thermal Processing, Pi et al., 2024), though it's worth noting that the evidence base here relies more on laboratory measurements than on formal oral food challenge data.
Peach and some nuts are the exception, not the rule. NSLTPs — the thermostable proteins found in peach (and present in certain nuts) — survive cooking and digestion. This is why peach, more than almost any other food on the cross-reactive list, occasionally causes reactions beyond the mouth: hives, abdominal pain, and in rare cases, systemic anaphylaxis. If you notice that peach reactions feel different — more intense, or involving your skin or gut — that's worth discussing with an allergy specialist. It doesn't mean cooking peaches is dangerous; it means the mechanism is different and warrants proper evaluation.
Reactions may be worse during peak pollen season. Several clinicians and observational studies have noted that PFAS symptoms can intensify when pollen counts are high — consistent with the idea that your immune system is already on high alert, with elevated circulating IgE. This isn't well-quantified in the literature yet, but it's a pattern many patients recognise intuitively.
OAS is not the same as a primary food allergy. The anxiety around PFAS is understandable — an itchy throat is alarming. But the mechanism is genuinely different from, say, a peanut allergy in a non-pollen-sensitised person. The proteins involved are fragile, the reactions are typically self-limiting, and the management is largely about awareness rather than strict avoidance.
The Evidence Landscape: What We Know, and What We Don't
The birch-food cross-reactivity picture is the most robustly established, with moderate-to-high confidence based on mechanistic studies, clinical cohort data, and molecular characterisation of allergens. Grass pollen cross-reactivity is somewhat less well-characterised by large prospective studies, though the molecular mechanisms — particularly for profilins — are well understood.
Prevalence estimates for OAS in hayfever sufferers are imprecise. The 70% figure often cited for birch-sensitised individuals reflects clinical surveys rather than rigorously controlled studies. For grass pollen, estimates of 20–50% oral reactivity exist, but confirmed clinical rates are consistently lower. A 2024 Japanese prevalence survey and broader reviews (Haidar et al., 2024) suggest that roughly 10–50% of pollen-sensitised individuals experience some food cross-reactivity depending on geography, diet, and dominant local pollen — a wide range that honestly reflects how heterogeneous the research is (confidence: low for exact prevalence figures).
One important thing the evidence is clear on: avoiding cross-reactive foods during pollen season does not reduce your hayfever symptoms. This is a common assumption, but there is no RCT evidence supporting it. The oral mucosa reaction and the nasal airway inflammation are mechanistically separate processes. Your nose isn't getting worse because you ate a raw apple; and eating cooked apple instead won't make your eyes less itchy in May. Current allergy management guidelines do not recommend dietary elimination as a strategy for reducing rhinitis (Vieths et al., 2002; Bohle, 2007).
What remains genuinely unknown: whether cumulative allergen load from both inhaled and ingested cross-reactive proteins might worsen sensitisation over time; whether there are meaningful differences in PFAS severity by age, sex, or geographic region; and whether standard allergy immunotherapy for pollen has a meaningful downstream effect on food cross-reactivity (early data suggest it may, but this is not yet established).
What Haelo Recommends
Based on the evidence, here's how to approach PFAS practically:
1. Map your own pattern first. Not everyone who is pollen-allergic experiences PFAS, and which foods affect you depends on which pollens you're sensitised to. Keep note of which raw foods cause symptoms and in which season — this helps distinguish true food allergy from cross-reactivity, and helps you identify whether birch (spring) or grass (early summer) is your primary driver.
2. Cook it when in doubt. For most cross-reactive foods — apple, carrot, celery, melon, tomato — cooking thoroughly eliminates the problem. This is not avoidance; it's preparation. You don't need to remove these foods from your diet.
3. Treat peach (and stone fruits) with slightly more caution. If symptoms from peach or other stone fruits ever go beyond the mouth — hives, stomach cramps, feeling faint — stop eating the food and seek medical advice. NSLTPs behave differently and warrant a proper allergy evaluation.
4. Don't restrict your diet unnecessarily during pollen season. There's no evidence that avoiding cross-reactive foods reduces hayfever. Unnecessary dietary restriction during an already difficult season adds burden without benefit.
5. Mention it to your GP or allergist. PFAS is widely under-recognised and under-discussed in primary care consultations. If you've experienced these symptoms, naming them — and understanding their cause — opens up better conversations about your overall allergy management, including whether immunotherapy might be right for you.
6. Watch for seasonal intensification. If you notice raw food reactions feel worse during peak pollen weeks, that's consistent with what we understand about IgE dynamics during high-exposure periods. It's not a sign something new is wrong — it's your immune system responding to a cumulative load. This is exactly the kind of pattern Haelo is built to help you track and anticipate.
The science of cross-reactivity is still maturing, and Haelo will continue to update its guidance as the evidence evolves. What we know already is enough to make your season meaningfully more manageable — and to stop you worrying unnecessarily about apples.
The evidence
What the research actually says
Each answer below is drawn from a graded research review. Confidence reflects the strength of the underlying evidence, not how confident we feel about it.
Which foods cross-react with grass pollen allergens?
Grass pollen allergens most commonly cross-react with foods in the melon family (cantaloupe, watermelon, honeydew), tomatoes, potatoes, oranges, peaches, celery, peanuts, and kiwi, producing pollen-food allergy syndrome (PFAS) or oral allergy syndrome (OAS) in sensitized individuals. Reactions are typically mild and localized to the oropharynx due to heat-labile proteins denatured by cooking or digestion, though LTP-mediated reactions (e.g., peaches) can occasionally trigger systemic anaphylaxis. An estimated 20–50% of grass pollen-allergic individuals report oral symptoms upon ingesting implicated raw foods, though confirmed clinical reactivity rates are lower.
How it works
Cross-reactivity is driven primarily by structural homology between grass pollen pan-allergens—particularly profilins (e.g., Phl p 12 from timothy grass, sharing >70% sequence identity with food profilins in melons, tomatoes, and peanuts)—and homologous proteins in plant foods, triggering IgE-mediated mucosal responses following prior inhalational sensitization. Non-specific lipid transfer proteins (nsLTPs, e.g., Phl p 14) represent a secondary but clinically significant mechanism, as their thermostability and digestion resistance underlie more severe reactions associated with fruits such as peaches.
Confidence: moderate
Which foods cross-react with birch pollen allergens?
Birch pollen allergens, particularly Bet v 1 (a PR-10 pathogenesis-related protein), cross-react with homologous proteins in a wide range of foods including Rosaceae fruits (apple, pear, peach, cherry), Apiaceae vegetables (carrot, celery), nuts (hazelnut, almond), and legumes (soy, peanut), causing pollen-food allergy syndrome (PFAS)/oral allergy syndrome (OAS) in an estimated 70% of birch-sensitized individuals. Secondary cross-reactivity via Bet v 2 (profilin) occurs in approximately 10-15% of birch-allergic patients and broadens the implicated food spectrum. Reactions are typically mild and localized to the oropharynx due to the heat-labile nature of these proteins, which are degraded by cooking and gastric digestion.
How it works
IgE antibodies raised against Bet v 1 recognize structurally homologous PR-10 proteins in foods (e.g., Mal d 1 in apple, Cor a 1 in hazelnut, Gly m 4 in soy, Ara h 8 in peanut) due to high amino acid sequence identity (>40-60%), triggering mast cell degranulation at oral mucosal surfaces. Cross-reactive T-cell responses to these food homologues, as demonstrated for Bet v 1 and Mal d 1, further amplify and sustain the allergic sensitization.
Confidence: high
How common is oral allergy syndrome in hayfever sufferers?
Oral allergy syndrome (OAS) affects approximately 8.8–9.1% of children with allergic rhinitis based on pediatric cross-sectional data, though estimates in adult hayfever sufferers vary considerably by population, pollen sensitization profile, and region. A 2024 Japanese prevalence survey specifically in seasonal allergic rhinitis patients and broader reviews suggest rates may range from roughly 10–50% in pollen-sensitized individuals, with the wide range reflecting geographic differences in pollen exposure and dietary habits. The birch-apple syndrome is considered the prototypic form, but regionally dominant pollens (e.g., oak, grass, olive) shape which foods trigger reactions.
How it works
OAS is driven by IgE-mediated cross-reactivity between structurally homologous proteins in airborne pollen (e.g., Bet v 1 in birch, profilins) and heat-labile counterparts in raw plant foods, causing localized oropharyngeal symptoms that typically resolve because these allergens are rapidly degraded by gastric acid and proteases before systemic absorption.
Confidence: low
Does cooking or processing eliminate cross-reactive food allergens?
Thermal and non-thermal food processing can significantly reduce allergenicity by denaturing proteins and disrupting IgE-binding epitopes, but complete elimination of cross-reactive allergens is rarely achieved. Effectiveness varies markedly by food type and processing method: tree nuts (walnut, hazelnut, almond) and many legume allergens show high heat stability with persistent antibody reactivity, while labile allergens such as PR-10 proteins (e.g., Bet v 1 homologs in apple and carrot) are more readily destroyed by cooking. Peach represents a notable exception where processing can produce a nearly hypoallergenic product, but this remains the exception rather than the rule.
How it works
Thermal processing induces protein denaturation, Maillard reactions (glycation of lysine residues), and aggregation, which alter or mask conformational and linear IgE-binding epitopes, reducing immune recognition. However, allergens with stable disulfide-bonded or seed-storage protein structures (e.g., 2S albumins like Ara h 2, vicilins, legumins) maintain their tertiary structure and epitope accessibility even after extensive heating, explaining their persistent allergenicity post-processing.
Confidence: moderate
Can avoiding cross-reactive foods during pollen season reduce symptoms?
No high-quality clinical evidence (RCTs or systematic reviews) demonstrates that avoiding cross-reactive foods during pollen season reduces allergic rhinitis or hayfever symptoms. Cross-reactive food avoidance is supported only for preventing pollen-food allergy syndrome (PFAS) oral symptoms—such as lip swelling, oral itching, and throat irritation—which affect 20-70% of pollen-sensitized patients. Current management guidelines do not recommend dietary elimination as a strategy for reducing systemic pollen-driven nasal symptoms.
How it works
PFAS occurs when pollen-specific IgE antibodies (e.g., against birch Bet v 1) cross-react with homologous proteins in raw fruits, vegetables, and nuts (e.g., Mal d 1 in apples), triggering localized mast cell degranulation primarily in the oral mucosa. This local IgE-mediated reaction is distinct from the systemic airway inflammation driving rhinitis, and cooking denatures the relevant labile proteins, abolishing cross-reactivity—indicating no mechanistic pathway by which dietary avoidance would reduce pollen-induced nasal inflammation.
Confidence: low
What is the clinical severity spectrum of oral allergy syndrome — how often does it progress beyond mild oral symptoms to systemic reactions?
Oral allergy syndrome (OAS/PFAS) predominantly presents with mild, self-limited oropharyngeal symptoms (itching, tingling, angioedema of lips, tongue, and throat), but systemic progression occurs in a clinically significant minority. Estimates suggest up to 9% of OAS patients may experience more severe food allergy symptoms and approximately 2% may develop anaphylaxis, though these figures lack robust prospective cohort validation. Sensitization to heat-stable allergens such as lipid transfer proteins (LTPs) and specific nut allergens is consistently associated with higher risk of systemic and anaphylactic reactions compared to the more common birch-pollen-related, thermolabile Bet v 1-like protein sensitizations.
How it works
Most OAS reactions remain localized due to rapid denaturation of thermolabile cross-reactive proteins (e.g., Bet v 1 homologs) by saliva, digestive enzymes, and heat, limiting systemic allergen absorption and confining IgE-mediated mast cell activation to the oropharyngeal mucosa. Heat-stable proteins such as LTPs and seed storage proteins resist denaturation, enabling gastrointestinal absorption and systemic allergen distribution, which facilitates progression to generalized allergic reactions or anaphylaxis.
Confidence: moderate
Does oral allergy syndrome severity worsen during peak pollen season compared to off-season?
Clinical consensus and observational reports consistently indicate that OAS symptoms worsen during peak pollen seasons, with patients tolerating cross-reactive foods off-season but reacting during high pollen periods; however, no peer-reviewed studies have directly quantified this seasonal variation using validated symptom scales or controlled designs. The available academic literature establishes the IgE-mediated cross-reactive mechanism underlying OAS and documents high prevalence among pollen-sensitized patients (37-75% in birch-allergic cohorts), but does not prospectively measure within-patient symptom severity across seasons. The seasonal worsening hypothesis, while biologically plausible and clinically accepted, currently rests on expert opinion and clinical observation rather than controlled evidence.
How it works
During peak pollen season, continuous aeroallergen exposure drives heightened systemic IgE sensitization to pollen proteins (e.g., birch Bet v 1), which increases cross-reactive IgE binding to homologous labile proteins in raw fruits and vegetables, amplifying mast cell degranulation in the oral mucosa. Off-season reduction in pollen exposure likely diminishes this priming effect, lowering the threshold for symptom-free food tolerance, though direct evidence for basophil or mucosal mast cell priming mechanisms in this seasonal context remains speculative.
Confidence: low
Which specific foods most commonly trigger the most severe oral allergy syndrome reactions in UK grass pollen-sensitised individuals?
In UK grass pollen-sensitised individuals, the most commonly reported OAS/PFAS triggers include melon, tomato, orange, kiwi, and raw potato, with cereals and soy also implicated; however, robust UK-specific quantitative prevalence data for grass-specific triggers is largely absent from the peer-reviewed literature. The BSACI 2022 guideline (Skypala et al.) represents the strongest UK-contextualised evidence, noting that trigger foods vary by pollen sensitisation profile and geography, but does not provide ranked severity data for grass-specific triggers. Severe reactions (anaphylaxis) occur in approximately 1.7% of PFAS episodes overall, with nuts and soy anecdotally associated with higher severity risk, though this is not confirmed specifically for grass-sensitised UK cohorts.
How it works
Cross-reactivity occurs primarily via shared profilin epitopes between grass pollen allergens (notably Phl p 12) and homologous proteins in foods such as melon, tomato, and orange, producing typically mild, heat-labile reactions; PR-10 homologs and, rarely, stable lipid transfer proteins (LTPs) may also contribute, with LTPs more strongly associated with systemic/severe reactions but predominantly in southern European rather than UK populations.
Confidence: low
Does heat-treating cross-reactive foods fully eliminate the allergenic epitopes responsible for oral allergy syndrome or merely reduce them?
Heat treatment substantially reduces but does not fully eliminate the allergenic epitopes responsible for oral allergy syndrome, primarily because thermal denaturation disrupts conformational (three-dimensional) epitopes of heat-labile proteins such as PR-10 homologs and profilins, while linear/sequential epitopes persist and retain partial IgE-binding capacity. Clinical and in vitro evidence consistently shows that cooking renders most OAS-triggering foods (e.g., apples, carrots) tolerable for the majority of patients, but a subset of sensitized individuals—particularly those with high specific IgE levels or sensitization to linear epitopes—may retain residual reactivity. Quantitative studies using ELISA and basophil activation assays estimate a 60–90% reduction in allergenicity under standard cooking conditions (100°C, 5–15 minutes), but not complete abolition.
How it works
The key OAS allergens (PR-10 proteins like Bet v 1 homologs, and profilins) are heat-labile proteins whose IgE-binding capacity depends predominantly on conformational epitopes maintained by tertiary protein structure; heating induces unfolding and aggregation that masks or destroys these conformational sites, while the shorter linear peptide sequences that constitute sequential epitopes are thermostable and remain accessible to IgE. This distinction explains why cooking reduces but cannot universally eliminate reactivity, with the degree of reduction further modulated by food matrix effects, processing temperature and duration, and inter-individual variation in sensitization profiles.
Confidence: moderate
Where the evidence runs out
Large-scale, prospective epidemiological studies specifically quantifying grass pollen PFAS prevalence and severity are lacking, with most data derived from observational case series, clinical charts, or reviews extrapolating from birch pollen literature. The strength of association for peanuts, wheat, and kiwi with grass pollen specifically—as opposed to other pollen sensitizations—remains incompletely characterized, and IgE-inhibition studies confirming molecular cross-reactivity for grass-specific nsLTPs are limited. Most evidence derives from European cohort studies and case series rather than large systematic reviews or RCTs, limiting generalizability across different geographic regions and pollen exposure patterns. The predictive value of molecular sensitization profiles (e.g., specific IgE to rBet v 1 or rBet v 2) for clinical food allergy severity—rather than mere sensitization—remains incompletely characterized, and prevalence data in non-European populations are sparse. No large-scale systematic review or meta-analysis specifically quantifying OAS prevalence in adult hayfever sufferers was identified, and available studies are predominantly single-center, pediatric, or regionally specific, limiting generalizability. Adult cohort data, standardized diagnostic criteria across studies, and multi-regional longitudinal designs are needed to produce reliable global prevalence estimates. Most evidence derives from in vitro IgE-binding assays (ELISA, Western blot) rather than clinical oral food challenge data, leaving uncertainty about whether laboratory-measured reductions in antigenicity translate to reduced symptoms in hayfever patients with pollen-food allergy syndrome. Specific studies examining how processing affects labile PR-10 or profilin cross-reactive epitopes relevant to birch-pollen–related oral allergy syndrome (e.g., in apple, hazelnut, carrot) in clinically relevant doses are largely absent from the current evidence base. No RCTs or controlled trials have tested whether dietary elimination of cross-reactive foods measurably reduces hayfever symptom scores (e.g., TNSS) during pollen season, and it remains unclear whether cumulative allergen load from both inhaled and ingested cross-reactive proteins could additively worsen systemic sensitization over time. The potential bidirectional amplification between pollen exposure and PFAS severity—suggested by seasonal IgE monitoring studies—also warrants prospective investigation. Robust prospective cohort data quantifying exact rates of systemic progression stratified by specific pollen-food sensitization profiles, allergen source, and patient characteristics are lacking, with the AAAAI surveys and existing reviews noting that accurate epidemiological statistics on PFAS severity spectra remain unavailable. It is also unclear whether clinical or serological markers (beyond LTP sensitization) can reliably predict which patients will progress beyond localized symptoms, and longitudinal studies tracking OAS severity over time are scarce. No prospective or controlled studies exist that directly compare OAS symptom severity (using validated scales such as VAS or standardized oral food challenge outcomes) during peak versus off-peak pollen seasons with concurrent pollen count measurements, leaving the seasonal worsening hypothesis unquantified. Critical missing data include longitudinal symptom diaries, IgE titer fluctuations across seasons, and dose-response relationships between ambient pollen counts and OAS reaction thresholds. No peer-reviewed UK cohort studies using component-resolved diagnostics (e.g., specific IgE to Phl p 12 vs. food profilins) exist to quantify prevalence or rank severity of individual food triggers specifically in grass-sensitised individuals, and anaphylaxis rate data is not disaggregated by pollen type or specific food in available sources. The question of which foods cause the *most severe* reactions in this population remains unanswered by high-quality evidence, with existing guidance based largely on expert consensus and clinical observation rather than systematic data collection. Direct clinical trials specifically comparing raw versus heat-treated foods in pollen-sensitized OAS patients (e.g., birch-apple syndrome with Mal d 1 post-roasting) are largely absent, with most mechanistic data extrapolated from egg and milk allergy models that may not fully represent PR-10 and profilin behavior. Component-resolved quantification of residual sIgE binding to specific OAS allergens after standardized cooking protocols, alongside patient-level oral food challenges, is needed to define the clinical threshold of residual allergenicity and identify which patient subgroups remain at risk despite cooking.
References
- 1.Haidar L, Bănărescu C, Uța C · 2024 · Pollen–Food Allergy Syndrome: Allergens, Clinical Insights, Diagnostic and Therapeutic Challenges
- 2.Bohle B · 2007 · The impact of pollen-related food allergens on pollen allergy
- 3.Fritsch R, Bohle B, Vollmann U et al. · 1998 · Bet v 1, the major birch pollen allergen, and Mal d 1, the major apple allergen, cross-react at the level of allergen-specific T helper cells
- 4.Vieths S, Scheurer S, Ballmer-Weber B · 2002 · Current Understanding of Cross-Reactivity of Food Allergens and Pollen
- 5.Vieths S · 1997 · Allergenic cross-reactivity, food allergy and pollen
- 6.Pi X, Zhu L, Liu J et al. · 2024 · Effect of Thermal Processing on Food Allergenicity: Mechanisms, Application, Influence Factor, and Future Perspective
- 7.Bindslev-Jensen C · 1993 · Cross-reactivity in food allergy
This article is general information about hayfever, not medical advice. It should not replace guidance from your GP, pharmacist or allergy specialist — particularly if you are pregnant, treating a child, or managing asthma alongside hayfever. Read our medical disclaimer.
